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UniProt_function_text_descriptions

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Q9Z9J7
RS5_HALH5
Small ribosomal subunit protein uS5 (30S ribosomal protein S5)
MRRIDPNTLELEEKVVAINRVAKVVKGGRRFRFAALVVVGDKNGRVGFGMGKAQEVPEAIRKAVEDAKKNLIEVPIVGTTIPHEIVGRFGAGRVLLKPASEGTGVIAGGPVRAVLDLAGVGDILSKSLGSNNPINMVRATVKGLQELKRAEDVAKLRGKTVEELLG
With S4 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000255|HAMAP-Rule:MF_01307}.
Q9Z9J8
RL18_HALH5
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
MITKPIKNVARKKRHAHVRRTITGTPERPRLNVFRSSKHIYAQLIDDVNGVTVAAASSLDKELKLENGGNVEAAKKVGELVAKRALEKGYKTIVFDRGGYVYHGRVASLADAAREAGLQF
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}.
Q9Z9J9
RL6_HALH5
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
MSRIGNKPVEIPSGVTVTVNGADVTVKGPKGELKRTFNPEIVVKVEDNTVVVERPSDKKEHRALHGTTRSLISNMVEGVSKGFEKSLELVGVGYRAQKSGQKLVLNVGYSHPVEIVPEKGIEIEVPSNTKVTVKGIDKERVGAVASNIRSVRLPEPYKGKGIRYEGEYVRRKEGKTGK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
Q9Z9K0
RS8_HALH5
Small ribosomal subunit protein uS8 (30S ribosomal protein S8)
MVMTDPISDMLTRIRNANTVRHEKLELPASKIKKEIAEILKREGFIRDYEYIEDSKQGVIRIFLKYGSSNERVITGLKRISKPGLRVYAKAGELPRVLGGLGIAIVSTSKGVMTDKEARQQQVGGEVLAYVW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
Q9Z9K1
RS14Z_HALH5
Small ribosomal subunit protein uS14 (30S ribosomal protein S14 type Z)
MAKKSMIAKQKRTQKYKVREYTRCERCGRPHSVMRKFKLCRICFRELAYKGQIPGVKKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}.
Q9Z9K2
RL5_HALH5
Large ribosomal subunit protein uL5 (50S ribosomal protein L5)
MNRLKEKYQKEIVPSLTEKFNYSSVMAVPKLEKIVVNMGVGDAVQNAKALDKAVEELTEITGQKPIITKAKKSIAGFKLREGMPIGAKVTLRGERMYEFLDKLISVSLPRVRDFRGISKKAFDGRGNYTLGVKEQLIFPEIDYDKVDKVRGMDVVIVTTASTDEEARELLSQMGMPFQK
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement. Contacts the P site tRNA the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}.
Q9Z9K3
RL24_HALH5
Large ribosomal subunit protein uL24 (50S ribosomal protein L24)
MHVKKGDTVKVISGKDKGKQGVILEAYPKKDRVLVEGVNIVKKHAKPSQENPQGGILNMEAPIHVSNVLPIDPKTGEPTRVGYKVENGKKVRIAKKSGEVLDK
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
Q9Z9K4
RL14_HALH5
Large ribosomal subunit protein uL14 (50S ribosomal protein L14)
MIQQESRLKVADNSGARELLCIKVLGGSGRKTANIGDVIVCSVKQATPGGVVKKGDVVKAVIVRSKSGVRRNDGSYIKFDENAAVIVRDDKSPRGTRIFGPVARELRDNQFMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
Q9Z9K5
RS17_HALH5
Small ribosomal subunit protein uS17 (30S ribosomal protein S17)
MERNQRKVYTGRVVSDKMDKTITVLVETYKKDRLYGKRVKYSKKFKAHDENNSAKIGDIVRIQETRPLSKDKHFRLVEIVEEAVII
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}.
Q9Z9K7
RL16_HALH5
Large ribosomal subunit protein uL16 (50S ribosomal protein L16)
MLMPKRVKFRREHRGKMRGRAKGGTEVHFGEYGLQALEASWITNRQIEAARIAMTRYMKRGGKVWIKIFPSKPYTAKPLEVRMGSGKGAPEGWVAVVKPGKVMFEISGVSEEVAREALRLASHKLPVKCKFVKREEVGGDANEN
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
Q9Z9K8
RS3_HALH5
Small ribosomal subunit protein uS3 (30S ribosomal protein S3)
MGQKVNPVGLRVGVIRDWESKWYAEKDYADLLHEDIKIREYIENRLKDASVSKIEIERAANRVNITISTAKPGMVIGKGGSEVEALRKALNELTGKRVHINIFEVKQADLDAKLVAENIARQLENRISFRRAMKQAIQRTMRAGAQGIKTQVSGRLGGADIARAEHYSEGTVPLHTLRADIDYGTAEADTTYGKLGVKIWIYRGEVLPTKGKNKKEGGN
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-Rule:MF_01309}.
Q9Z9K9
RL22_HALH5
Large ribosomal subunit protein uL22 (50S ribosomal protein L22)
MQAKAVAKQVRIAPRKARLVIDLIRGKQVGEAIAILKHTPKAASPIIEKVLNSAIANAEHNYEMEPNNLVISEAFVDEGVTLKRFRPRAMGRASRINKRTSHITIVVTEKKEG
This protein binds specifically to 23S rRNA its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
Q9Z9L0
RS19_HALH5
Small ribosomal subunit protein uS19 (30S ribosomal protein S19)
MGRSLKKGPFVDDHLMKKIETLNESNDKKVVKTWSRRSTIFPEFVGHTIAVYDGRKHVPVYISEDMVGHKLGEFAPTRTYKGHAADDKKTRR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q9Z9L1
RL2_HALH5
Large ribosomal subunit protein uL2 (50S ribosomal protein L2)
MAIKKYKPTSAGRRGMSTLDFAEITTDKPEKSLLAPLHKKGGRNNQGKMTVRHQGGGHKRQYRIIDFKRNKDGIPGRVATIEYDPNRSANIALINYVDGEKRYILAPKGLKVGMTIESGPEADIKVGNALPLKNIPVGTVIHNIELKPGKGGQLVRSAGAEAQLLGKEGDYVLVRLNSGETRYILATCRATIGQVGNLEHELVNIGKAGRSRWLGKRPTVRGSAMNPNDHPHGGGEGRAPIGRKSPMSPWGKPTLGYKTRKKNKASDKYIVRRRKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
Q9Z9L2
RL23_HALH5
Large ribosomal subunit protein uL23 (50S ribosomal protein L23)
MSNARDVIKRPVITERSTEVMGDKKYTFEVDVRANKTQIKDAIEEIFDVKVAKVNTMNYKGKPKRFGRYTGFTARRKKAIVTLTPDSKELDFFEGV
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
Q9Z9L3
RL4_HALH5
Large ribosomal subunit protein uL4 (50S ribosomal protein L4)
MPKVALYNQAGSQVGDIELSDAVFGIEPNENVLHDAVVMQQASLRQGTHKTKTRSEVRGGGRKPWRQKGTGRARQGSIRSPQWVGGGTVFGPTPRSYSYKLPKKVRRLAIKSALSSKVKAEEIVVLESLALEAPKTKEMASILSGLSVDRKALVVTADYNDNVALSARNIPGVTFVTAEGVNVLDVIKHDKLIITKDAVEKVEEVLA
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of the polypeptide exit tunnel. {ECO:0000255|HAMAP-Rule:MF_01328}.
Q9Z9L4
RL3_HALH5
Large ribosomal subunit protein uL3 (50S ribosomal protein L3)
MSKGILGKKVGMTQVFAENGDVIPVTVIEAAPNVVLQKKTVDSDGYEAVQLGFDDQKQNNANKPEKGHAAKAETAPKRFIKEIRGVNLDEFEVGQEIKVDAFAEGDIVDVTGTSKGKGFAGAIKRHNQARGPMSHGSRYHRRPGSMGPVDPNRVFKGKALPGRMGGEQVTVQNLEIIKVDAERNLLLVKGNVPGAKKSYVTVRSAIKSK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
Q9Z9L5
RS10_HALH5
Small ribosomal subunit protein uS10 (30S ribosomal protein S10)
MAKQKIRIRLKAYDHRVLDQSAEKIVETAKRSGANVSGPIPLPTEKSVYTILRAVHKYKDSREQFEMRTHKRLIDIVNPTPQTVDALMRLDLPSGVDIEIKL
Involved in the binding of tRNA to the ribosomes. {ECO:0000255|HAMAP-Rule:MF_00508}.
Q9Z9L6
EFTU_HALH5
Elongation factor Tu (EF-Tu)
MAKEKFDRSKTHANIGTIGHVDHGKTTLTAAITTVLAKRSGKGVAMAYDAIDGAPEERERGITISTAHVEYETDNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRQVGVPYLVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIRGSALKALEGDAEWEEKIIELMAAVDDYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQLNVGDEVEIIGLEEEAKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEVQRGQVLAKPGTITPHTNFKAEVYVLSKEEGGRHTPFFSNYRPQFYFRTTDVTGIIQLPDGVEMVMPGDNVEMTVELIAPIAIEEGTKFSIREGGRTVGAGVVASIQK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
Q9Z9L7
EFG_HALH5
Elongation factor G (EF-G)
MAREFSLENTRNIGIMAHIDAGKTTTTERILFYTGRIHKIGETHEGASQMDWMEQEQERGITITSAATTAQWKNNRINIIDTPGHVDFTVEVERSLRVLDGAVAVLDAQSGVEPQTETVWRQATTYGVPRVVFVNKMDKTGADFLYSVSTLHDRLQANAHPIQLPIGAEDNFEGIIDLVDMVAYFYEDDLGTRTEAKEIPDEYKEQAQEYHEKLVEAAAELDEELMMKYLEGEELTKDELKAAIRKGTCNVEFYPVLCGSAFKNKGVQLMLDAVLDYLPSPLDVPAIKGHVPDTEEEAVRKPGDDQPFAALAFKVMTDPYVGKLTFFRVYSGTLDSGSYVKNSTKDKRERVGRILQMHANHREEISTVYSGDIAAAVGLKDTSTGDTLCDEKNLVILESMEFPEPVIHLSVEPKSKADQDKMGLALAKLAEEDPTFKTHTDEETGQTIIAGMGELHLDIIVDRLRREFKVEANVGAPQVSYRETIRQAAQVEGKFVRQSGGRGQYGHVWIEFSPNEEGAGFEFVNGIVGGVVPREYIPSVQAGLEEALENGLLAGYPVIDIKAKLFDGSYHDVDSSEMAFKIAASMALKNAKSKCNPVLLEPMMKVEVVVPEEYMGDVMGDITSRRGRVEGMEARGNAQVVKAFVPLAEMFGYATSLRSRTQGRGTYTMFFDHYEEVPKSISEEIIKKNSGE
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Q9Z9L8
RS7_HALH5
Small ribosomal subunit protein uS7 (30S ribosomal protein S7)
MPRKGPVARRDVLPDPIYNSKLVTRLINRIMVDGKRGIAQKILYNAFELVRERSGKDPMEVFDQALKNIMPVLEVKARRVGGANYQVPVEVKPERRTTLGLRWLVNYSRLRGEKTMEERLANEILDAANNTGAAVKKREDTHKMAEANKAFAHYRW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. {ECO:0000255|HAMAP-Rule:MF_00480}.
Q9Z9P4
TATC_HALH5
Sec-independent protein translocase protein TatC
MNERDMSLMDHIAELRRRILIIVVFFVIALVVGFFLATPMITYLQGAPTAQDLPMNAFKLTDPLRVYMTFAFTSAFILVFPIILYQLWAFVSPGLHENERKATLAYIPIAFFLFLGGLSFAYFILFPFLIQFIGGLAERLHINELYGINEYFTFLFQITMPFGVLFQLPVVVMFLTRLGIVTPEFLRSVRKYAFFVLLVVAGFITPPELISHLMVTVPLLLLYEFSIWVSHLTYRKVQKLEKLRQEEYRQEEG
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. {ECO:0000255|HAMAP-Rule:MF_00902}.
Q9Z9P6
REX_HALH5
Redox-sensing transcriptional repressor Rex
MNNEPTKIPQATAKRLPLYYRFLENLHASGKQRVSSSELSEAVKVDSATIRRDFSYFGALGKKGYGYNVNYLLTFFRKTLHQDELTKVMLIGVGNLGTALLNYNFSKNNHTQIVMAFDVDREKIGNTVSGVKIENLDNLENKITSDVSVAILTVPAAVAQKTADRLVNAGVKGILNFTPARIAVPEHVRVHHIDLSVELQALIYFLKHYPL
Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. {ECO:0000255|HAMAP-Rule:MF_01131}.
Q9Z9T7
MMGF_HALH5
2-methylisocitrate lyase (2-MIC) (MICL) (EC 4.1.3.-)
MAWIVEQPKSQKELADRFRQLMKEEAILQIPGAHDAMAALVAKKAGFSALYLSGDAYTASRGLPDLGIVTSTEVADRAKDLVRATNLPVLVDIDTGFGGVLNVARTAQEMLEANVAAVQIEDQQLPKKCGHLNGKQLVSKEEMEQKIQAIKKVAPTLVIVARTDARANEGLNGAIERANVYIEAGADAIFPEALQSAEEFRLVAENVSAPLLANMTEFGKTPLMTAGGLQNAGFQMVIYPVTSLRVAAKAYERIFQLIKDEGTQEAGIEDMQTRKELYETISYDDFEALDKNIAKTVLGE
Involved in the methylcitric acid cycle. Catalyzes the cleavage of 2-methylisocitrate to yield pyruvate and succinate.
Q9Z9W9
GATA_HALH5
Glutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A) (EC 6.3.5.7)
MSLFDLKLKDVHTKLHEKEISVSDLVDEAYKRIEQVDGQVEAFLALNEEKARAYAKELDAALDRSEARGLLFGIPIGVKDNIVTKNLRTTCSSRILGNFDPIYDATVVHKLREAQAVTIGKLNMDEFAMGSSTENSAFQKTKNPWNLEYVPGGSSGGSAAAVAAGEVPFTLGSDTGGSIRQPAAYCGVVGLKPTYGRVSRYGLVAFASSLDQIGPITRNVEDNAYLLQAISGHDPMDSTSANLDVPDYLSALTGDIKGLKIAVPKEYLGEGVKEEVKQSVLDALKVLEGLGATWEEVSLPHSKYALATYYLLASSEASANLARFDGVRYGFRSDNADNLLDMYKQTRAEGFGDEVKRRIMLGTFALSSGYYDAYYKKAQQVRTLIKQDFEKVFEQYDVIIGPTTPTPAFKIGEKTDDPLTMYANDILTIPVNLAGVPAISVPCGFDNGLPLGLQIIGKHFDEGSVYRVAHAFEQATDYHTKRPTL
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
Q9Z9X0
GATB_HALH5
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-)
MNFETVIGLEVHVELKTESKIFSASPNHFGAEPNANTSVIDLGYPGVLPVLNKAAVEFAMKAAMALNCEVATDTKFDRKNYFYPDNPKAYQISQFDKPIGENGWIEIEVDGTKKKIGITRLHLEEDAGKLTHSGNGYSLVDFNRQGTPLIEIVSEPDIRTPQEAYAYLEKLKSIIQYTGVSDCKMEEGSLRCDANISLRPVGQEEFGTKTELKNLNSFNFVRKGLEYEEKRQAQVLLSGGEILQETRRYDEAANKTVLMRVKEGSDDYRYFPEPDLVALHIDDEWKARIRSEIPELPDARKKRYVEELGLPAYDAMVLTLTKEMSDFFEETIAKGADPKLASNWLMGEVSGYLNAEQKELDEVALTPDGLAKMIQLIEKGTISSKIAKKVFKDLIEKGGDPEEIVKAKGLVQISDEGELRKYVVEVLDNNQQSIDDFKNGKDRAIGFLVGQIMKATKGKANPPMVNKLLLEEINKR
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Q9ZA15
SSI_STRFR
Subtilase-type protease inhibitor
MRNRAKTALVGTLVAATAALGPLGGTAHAGDSSLYAPSDLVLTIAHGEDAASVAPERAVTLTCEPQARGTHPSPQEACVLLGDAGGDVDAIAPPAEPQLCTYQYDPVVVTCXGVWQGRFVDQERTFGNECVMRAETGAVFDF
Strong inhibitor of bacterial serine proteases such as subtilisin.
Q9ZA86
PTSO_PROMH
Phosphocarrier protein NPr (Nitrogen-related HPr)
MTQYRRVAIKNRLGMHARPAMKLFDLVNTFQSTVTLRNHEGVEAQADSVIAMLMLDSEQGSHIDIEASGCDEKEAIDAIIALFESGFDED
Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins.
Q9ZA87
RAPZ_PROMH
RNase adapter protein RapZ
MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVDLLPELAKTLAERDAAAAAVSIDVRNMPESPEIFEKALESLPAEYSPQLLFLDADRNTLIRRYSDTRRLHPLSTKNLSLEMAIDTESDLLEPLRSRADLIIDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDRPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYVAEQLADYFRSRGKNVQSRHRTLEKRK
Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. {ECO:0000255|HAMAP-Rule:MF_00636}.
Q9ZAA0
PQQA_PSEAE
Coenzyme PQQ synthesis protein A (Pyrroloquinoline quinone biosynthesis protein A)
MWTKPSFTDLRLGFEVTLYFANR
Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide (By similarity).
Q9ZAA1
ACLDH_PSEAI
Acetaldehyde dehydrogenase (EC 1.2.1.-)
MIYAAPGTPGAVVTFKPRYGNYIGGEFVPPVKGQYFTNTSPVNGQPIAEFPRSTAEDIDKALDAAHAAADAWGRTSVQERSNILLKIADRIEQNLELLAVTETWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPLGICVLLELIGDLLPPGVLNVVQGFGREAGEALATSKRIAKIAFTGSTPVGSHILKCAAESIIPSTVELGGKSPNIYFEDIMQAEPAFIEKAAEGLVLAFFNQGEVCTCPSRALVQESIYPAFMEEVLKKVRAIKRGDPLDTETMVGAQASQQQYEKILSYLDIAQQEGAELLAGGSVEKLEGNLASGYYIQPTLLKGHNGMRVFQEEIFGPVVGVTTFKDEAEALAIANDTEYGLGAGLWTRDINRAYRMGRGIKAGRVWTNCYHLYPAHAAFGGYKKSGVGRETHKMMLDHYQQTKNLLVSYDIDPLGFF
Catalyzes the NAD(+)-dependent oxidation of acetaldehyde to acetate. Is likely a component of the ethanol oxidation system that allows P.aeruginosa to grow on ethanol as the sole carbon and energy source.
Q9ZAD9
PTHP_LACLC
Phosphocarrier protein HPr (Histidine-containing protein)
MASKEFHIVAETGIHARPATLLVQTASKFTSEITLEYKGKSVNLKSIMGVMSLGVGQGADVTISAEGADADDAIATIAETMTKEGLAE
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
Q9ZAE3
RL18_THEMA
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
MIKKESKKEQRLRRHRRVRKKVFGTPERPRLCVFRSNKHIYAQIIDDTIGHTLVSASTLDPELREKLQKTWNVEAAKEVGLLIGKRALEKGIKKVVFDRGGYKYHGRVKALADGAREAGLEF
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}.
Q9ZAE4
RL6_THEMA
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
MSRLAKKPIVLPQGVTVEIKDNVVKVKGPKGELSQEFLPYVKIEVEGNEVWVRPNEEQIIRKSDWRKVKMFQGTYWSLIRNMVVGVTEGYKKELEIVGIGYRAQLQGNTLVMNLGYAHPVVYEIPSDVKIEVPAPNRIIVSGIDKQRVGQVAAEIRAFRPPNVYTGKGIRYVGEVVRQKEGKKA
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
Q9ZAE5
RS8_THEMA
Small ribosomal subunit protein uS8 (30S ribosomal protein S8)
MWSDPIADMLTRIRNANMVFKEYTDIPASNLKKKICEILKREGFIADYKYIEDGKQGILRVYLKYKGGRKNRERVIHGIVRVSHAGRRIYVDKDHIPKVKNGLGIAILTTSKGVLTDKEARQLGVGGEVIAYVW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
Q9ZAE6
RS14Z_THEMA
Small ribosomal subunit protein uS14 (30S ribosomal protein S14 type Z)
MAKKAMIERWKKPKKYKVREYTRCHICGRPRAVYREFGLCRICFRKLALEGKLPGVRKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}.
Q9ZAH3
RS6_CAMJE
Small ribosomal subunit protein bS6 (30S ribosomal protein S6)
MKHYEVLFILKPTLTEEEVNTKLEFVKEVLTKNSAEIETVVPMGTRKLAYKIKKYERGTYFVIYFKAPTNLIAELERVLRITEEVIRFLIVKYENKKEIAAWEKLSHGIKQSKKEIKPLDAPEIQ
Binds together with bS18 to 16S ribosomal RNA.
Q9ZAH6
ACPS_STAA8
Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
MIHGIGVDLIEIDRIQALYSKQPKLVERILTKNEQHKFNNFTHEQRKIEFLAGRFATKEAFSKALGTGLGKHVAFNDIDCYNDELGKPKIDYEGFIVHVSISHTEHYAMSQVVLEKSAF
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
Q9ZAI9
SEPF_LACLM
Cell division protein SepF
MAFKDWMNNLRDYFVEDDEEFNEPTRPVQESRPTVASTPKPKVEERKVQADYQSRRPAQTTPKPQTQTAAPKRSASTFSKPMPEKIVQQQTVSQAQSLAATVSTIAIKEPRAYADIMESARIVKNGECVLVNFKFMGDAQARRSIDFMTGVVFTLDGDIQNVGGQIFLMTPANITVDAAKEMSILAGQNFESYDIY
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. {ECO:0000255|HAMAP-Rule:MF_01197}.
Q9ZAQ8
SSB_CERS4
Single-stranded DNA-binding protein (SSB)
MAGSVNKVIIIGNLGRDPEVRSFQNGGKVVNLRIATSEQWRDRASGERKERTEWHSVAIFDENLARVAEQYLRKGSTVYIEGQLETRKWQDQSGQDRYSTEVVLRPFRSSLTMLGGRGEGAGAGGGMGGGGYEDRGGPDNYDNYGSGPRGGASSGGAPSGGGRRNDLDDEIPF
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. {ECO:0000255|HAMAP-Rule:MF_00984}.
Q9ZAU1
DNRU_STRPE
Putative daunorubicin C-13 ketoreductase DnrU (EC 1.1.1.-)
MTASTPHHGTPRGGLSGRTVLVTGATSGIGRAAALAVARQGARVVLVGRDPERLRTVTNEVARTAGPAPDAFRADFAELRQVRDLGERLRDRYPRIDVMASNAGGMFWSRTTTQDGFEATIQVNHLAGFLLARLLRERLAGGRLILTSSDAYTQGRIDPDDLNGDRHRYSAGQAYGTSKQANIMTAAEAARRWPDVLAVSYHPGEVRTRIGRGTVASSYFRFNPFLRSAAKGADTLVWLASAPAEELTTGGYYSDRRLSPVSGPTADAGLAAKLWEAGAAAVGDTAH
Could reduce the 13-carbonyl of daunorubicin to yield (13S)-13-dihydrodaunorubicin. Could also be able to reduce the 13-carbonyl of doxorubicin.
Q9ZAU2
DNRV_STRPE
Anthracycline biosynthesis protein DnrV
MTRFAPGAPAWFDLGSPDVAASADFYTGLFGWTATVVSDPGAGGYTTFSSDGKLVAAVARHQIDTPYHRPYGPGNDQHGMPAIWTVYFATDDADALTKRVETAGGEVIMTPMDVLGLGRMAVFADPAGAAFAVWRKGVMEGAEVTGVPGSVGWVELVTDGIGAARDFYPATLGLAPADTGLKGVTDPVWHIGDTPVAGTQELGVTGAVRPHWAVLFAVHDCDATVRRAVELGGSVENEPADTPRGRRADLLDPHGAGFSVVELREGYPAAAGGAS
Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, it acts jointly with DoxA in the conversion of 13-deoxycarminomycin and 13-deoxydaunorubicin to yield carminomycin and daunorubicin, respectively. In vitro, it also acts jointly with DoxA in the C-14 hydroxylation of daunorubicin to form doxorubicin, although this strain is not a doxorubicin producer.
Q9ZB11
GALR_STRTR
HTH-type transcriptional regulator GalR (Galactose operon repressor)
MATLADIAKLAGVSISTVSRVLNKDETLSVTEDTRHRILTIADEIGYTKYKTINNSKKEKYQVAIIQWVSEEHELDDIYYYNIRLGIEKRAYELDYEMLHFFNDIPSSLGEEVVGVLCIGKFSREQIAKLERLKKTLVFVDSDTLNQGHPCVTTDFENSVQSALCYLKEQGCNNIGLLIGQEKTTDATEIISDPRLRSYRNYCMEKGIYDPLFILTGDFTVQSGYELLDSKIKSGATLPDAYFAASDSLAIGALRALQENGIKVPDDIQIISFNDTTLAKQVYPPLSSVTVYTEEMGRTAMDILNKQLLAPRKIPTLTKLGTKLTLRNSTK
Repressor of the galactose operon. Binds galactose as an inducer (By similarity).
Q9ZB62
OTC_GEOSE
Ornithine carbamoyltransferase (OTCase) (EC 2.1.3.3)
MNAVMSLKGRDFLTLLDFSTEEILDLLALAADLKAKQKAGVSYTPLSGKTMAMIFEKPSGTRVSFEVGMIQLGGQAMYLNGNHLQLGRGETIADTARVLSQYVRVIMIRTFAHQKVEELAEYASFRSSNGLTDDDHPCQALADLLTIYEVKKTFQGVKLAYVGDGNNVANALLVAAAKVGMDVAIACPPGYEPKKEYVEAACRVGEQTGRRVTVTHDPLVAVAGADRIYTDVWTSMGQESESSERLQVFQPYQVNEELVKAAKPDYLFLHCLPAHRGEEVTAGVMDGPNSVVFEQAGNRLHAQKAILLSVL
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q9ZB76
YQGF_MYCGE
Putative pre-16S rRNA nuclease (EC 3.1.-.-)
MKYILAIDFGLKKIGTAIANTLDKYPSAFHVFEVKNNFKTAVNNLFLRIKNDGYELEKIVIGFPKFHYYSDIQKAIKSFKQLLEKRFNLPIILVDESNTTSAVKDKLITMDLKHKDFKKAKDTLAAVLILERFFQNYH
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}.
Q9ZB79
ACPS_MYCGE
Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
MVVGIGIDVVQLKRFLTLVETSDCFAKRLLTSNELNSYWKLNNNQRANFLAVHWTLKEAIYKATSHIKPLFTKLEIYKLNNQYRCEFIQNINLLLSVSYTNCHVSAICLAQQNG
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
Q9ZBH0
Y6443_STRCO
Putative S-adenosyl-L-methionine-dependent methyltransferase SCO6443 (EC 2.1.1.-)
MADTAPLGTRTDGVEGGVGLTALLVAAARAIETHRPDALAQDIYAEHFVLGARASAHWPVRLDRAPGGDTSPLWGRFARYFGLRTRVLDDFLLRSVRSAGIRQVVLLGAGLDARAFRLDWLSDCVIFEIDRDGVLAFKHRVLDTLSAEPGARRVPIGTDLRADWAGALTATGFDATAPTAWLVEGLLFYLPHAAETALIDTVDRLSAPGSALAYEVKLEKDLMAYRDSPLYVSTRRQLGIDLLDLFSREPRPDSAARLRDRGWTASVHTPFDFTRRHGRGPLPEENDALAGNRWVFADRARPA
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
Q9ZBH3
Y6440_STRCO
Putative (5-formylfuran-3-yl)methyl phosphate synthase (EC 4.2.3.153) (4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase) (4-HFC-P synthase)
MLLLISPDGVDEALDCAKAAEHLDIVDVKKPDEGSLGANYPWVIREIRAAVPADKPVSATVGDVPYKPGTVAQAALGAAVSGATYIKVGLYGCATPEQAVEVMRGVVRAVKDHRADAFVVASGYADAHRIGCVNPLSLPDIARRSGSDAAMLDTAIKDGTRLFDHVPPDVCAEFVRRAHDCGLLAALAGSVRSGDLGELARIQTDIVGVRGAVCEGGDRTTGRIRPHLVAAFRAEMDRHVREHAAAAAQS
Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Q9ZBS2
FBID_STRCO
Phosphoenolpyruvate guanylyltransferase (PEP guanylyltransferase) (EC 2.7.7.105)
MQWTLVVPVKALARAKSRLSDTADDGLRPGLALAFAQDTVAAALACPAVADVAVVTDDARAGRELAALGAGVVADEPGGGLNAALAHGAAVVRAARPESPVAALNADLPALRPAELARVLAAATQFPRAFLPDAAGIGTTLLTVAPGQELAPAFGADSRARHRASGAVELRLDAVDSVRQDVDTGGDLRSALALGVGPRTAAVAARLLIAGQ
Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. {ECO:0000255|HAMAP-Rule:MF_02114}.
Q9ZBW0
FDHD_STRCO
Sulfur carrier protein FdhD
MGRVTERRKVIRIRDGAVSTRPDTLVAEEPLEIRLNGKPLAITMRTPGDDFALAAGFLVSEGVLAEQRDLQNIVYCAGATVDGSNTYNVVDVKTAPGVRIPDITLERNVYTTSSCGLCGKASLDAVRTTARWPIADTPPVRVTPELLADLPDRLRASQRVFDRTGGLHAAALFTEDGELVDVREDVGRHNAVDKLVGRALQNADLPLSRSVLLVSGRASFELAQKAVMAGIPVLAAVSAPSSLAVDLAAETGLTLVGFLRGSSMNVYAGADRVALRAAVGQG
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. {ECO:0000255|HAMAP-Rule:MF_00187}.
Q9ZBX9
KPTA_STRCO
Probable RNA 2'-phosphotransferase (EC 2.7.1.-)
MQQERTVKVSKYLSKHLRHQPERIGLTPDEGGWVEIDALVAAAAAHGFPFTRQELDHVVATNDKRRFAVEGTRIRASQGHSIAVDLRLPVATPPPYLYHGTVARHLEAIRAEGLRPMNRHDVHLSPDRETATRVGARRGRPVVLPVDAATMHRDGHVFHVSANGVWLTQHVPSRYLRFPAPH
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By similarity).
Q9ZBY8
PATR_STRCO
Putative phenylalanine aminotransferase (EC 2.6.1.-)
MSETSPKLRAELEGIPTYKPGKPAAADGPVAYKLSSNENPYPPLPGVMETVTAAAASFNRYPDMACTSLMAELSDRFGVPLAHLATGTGSVGVAQQLIQATSGPGDEVIYAWRSFEAYPIITQISGARSVQVPLTPGEVHDLDAMADAITDRTRLIFVCNPNNPTGTVVRRAELERFLDRVPSDVLVVLDEAYREFIRDAEVPDGVEFYRERPNVCVLRTFSKAYGLAGLRVGFAIAHEPVAAALRKTAVPFGVSQIAQEAAIASLRAEDELIGRVGSLVCERARVADALRAQGWTVPESQANFVWLRLGERTLAFANACEQAGVVVRPFAGEGVRVTVGESEANDIFLKVSEEFRKEL
May catalyze the transamination reaction in phenylalanine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01513}.
Q9ZC08
GVPJ1_STRCO
Probable gas vesicle protein J1 (GvpJ1)
MTTPSRLPDPYGQGQSANLADILERVLDKGVVIAGDIKINLLDIELLTIKLRLVVASVDKAKEMGIDWWESDPALSSRARHDELTRENAALRERLRELDPGRVPREEAP
A minor component of the gas vesicle, might be involved in nucleating gas vesicle formation (By similarity). Gas vesicles (GV) are hollow, gas filled proteinaceous nanostructures. It is not clear what function GVs perform in soil bacteria (Probable).
Q9ZC13
GVPA1_STRCO
Gas vesicle protein A1 (GvpA1)
MTVVPAQQTGGGGSSGLYDVLELVLDRGLVIDAFVRVSLVGIEILKIDVRVVVASVDTYLRFAEACNRLDLEAGPRKDPGLPDLVGEMTESGARGKSKGALSGAAETISDAFKQARDDGGSERETSSRPRARKAAPSRRKEEQE
Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell (By similarity). It is not clear what function GVs perform in soil bacteria (Probable). {ECO:0000255|HAMAP-Rule:MF_00576, ECO:0000305}.
Q9ZC67
ASTA_YERPE
Arginine N-succinyltransferase (AST) (EC 2.3.1.109) (AOST)
MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. {ECO:0000255|HAMAP-Rule:MF_01171}.
Q9ZC68
ASTD_YERPE
N-succinylglutamate 5-semialdehyde dehydrogenase (EC 1.2.1.71) (Succinylglutamic semialdehyde dehydrogenase) (SGSD)
MSQHVMFNAVLSSHPALFIQGEWRIGNGVSFEKQDPMSQQRLWQARAADHTDVTLACHAARAAFPAWARASLEQRATVIQQFAALLEQHKQSLARTISLETSKPYWETLTEVQAMIGKVAISLQAYQTRTGHSQTPMGDSMSVLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWTAEETVKLWQQAGIPDGVLNLVQGGRETGEALAAQPDIDGLLFTGSAHTGYHLHRQLAGQPEKMLALEMGGNNALIVEQVKDRDAVVNLAIQSAFISAGQRCTCSRRLLVKTGAEGDAFLLRFTAVAQALRIGRWDEQPAPFMGAVISSQAAERMLAAQQHLLLLGGESLLNMTRPDSQSALLTPGIIDITNISEVPDEEYFGPLVSVIRYTDFTEALKIANQTRFGLAVGLVSEDRQQFEQLLLEARAGIVNWNKPLTGASSAAPFGGVGASGNHRPSAFYAADYCAWPMASLECEHLTLPATLSPGISFDLPKV
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. {ECO:0000255|HAMAP-Rule:MF_01174}.
Q9ZC88
MUTL_RICPR
DNA mismatch repair protein MutL
MTIKFLSESTINRIAAGEVIERPASVVKELVENAIDGGSTKIDIILERAGKNLIIVSDDGIGMTDKELEIAVKRHTTSKLNESDFFNIHTFGFRGEALASIAAISKMLITSKKREADKAFQIKLIGGNKQQITVSVHNEGTKIEVRDLFFATPARLKFLRSDKTELAASIDIVKKIALAHPRISFNLIHDNKNLLKLKGQNKDSETNLKQRIIDVIGDVFIKNAAYIDFKTPDFSICGYTSIPTYNKASSEDQFLFINNRPIKDKLLQVALRVAYQDYLARDRYALCVIFLQIDPQLVDVNVHPAKAEVRFHDPNYVRNILIEAIKNALTNKSQITATTIGSDKNSLVNKEPTIHKATNVNSKASEYTSFNFKRNTAYHTLPYGKIEQEVGKCIEHNNQSHKQYKFGVAKAQLHTTYIISQTEDSIVIIDQHAAYERLGYAKIKYCLKNGELVKQRLLIPEIVELSSQKKADCLYENREKLFKLSLTIEKFGEKSIIVTEIPNILGDVNVQKLIQDLADHLSDFAKNMPLKELIEHVIKIYICHYSIRAARKLSADEMNSLLRQMENMSFSAQCNNNRPTYIELKLKDIELLFRL
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).
Q9ZCA0
Y866_RICPR
Nucleoid-associated protein RP866
MVNFNQFLKQAQSMQKKMQEAQEQMANTRYTGKAGGMLVEIIITGKGEVEKISIDESLLKTEEKEMLEDLIKVAFNDAKQKCDEDSQNSLSGALNGMSLPPGFKIPF
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}.
Q9ZCB9
HTPG_RICPR
Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G)
MTQEKKKFDAEVGKILNLMIHSLYSNKEIFMRELISNASDACDKLRYLSQSNSELIAGDSNFKIIVKVDKDNGQIIIRDNGIGMNKEDLIENLGTIARSGTANFLKNLSGDSKKDNMLIGQFGVGFYSSFMVADKVTVTSRKAGESKVHTWESDGLGEYIVADSEQEFTRGTEIVLYIKKSETTFLDHFRLKHIVKSYSDHIAVPIYFCDEAGNNEIQLNSASALWTRPKSEITEDQYKEFYKSLSYAVDDPWVTLHNKNEGAIEFTNLLFIPSSKTFDLFHPDRKKRVKLYIKRVFISDENIDLIPSYLRFLRGVVDSEDLPLNISRESLQHNNVLEKIKNAITKRVLGELRKKKEELPEEYNKFWTNFGGALKEGLCEATTDHEKLLEVCIFRSALHNKMISIDEYIANFKEGQNTIYYLSGDNPDKLLSSPQIEGLLNKNIDVLLFTDTVDDFWVNVNSEYKGYAIKSATRSDIDVEQTTSQPKDKNTDSKKSDNEYKLLTDYFKEILGELVKEVKISKKLTLSPACLAVSDTAMDIRMERFLIEQKQIANASAKNLELNPKNKIIEKIFNDLKANNKNNNELVNLIFDQACILEGEPVADTGAFSKRLNDILQKAIL
Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00505}.
Q9ZCC2
SSB_RICPR
Single-stranded DNA-binding protein (SSB)
MAGSLNKVILIGNVGRDPEIRTTGEGKKIINLSLATTETWKDRITSERKERTEWHRVVIFSEGLVSIVERYVTKGSKLYIEGSLQTRKWNDNSGQEKYTTEVVLQNFNSQLILLDHKNSNQNTQGSGHHEYKYPETKNHSFDHSDLDDEIPF
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. {ECO:0000255|HAMAP-Rule:MF_00984}.
Q9ZCC8
FER_RICPR
Ferredoxin
MTYVVTDECVKCKYTDCVEVCPVDCFYEGEFMLVINPDECIDCGVCVPDCPIDAIKPESPELIEWVERAKDFIENHGWKNITKKKCALPGADKFKDEKDKFNKYIIKKT
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Q9ZCE0
XERC_RICPR
Tyrosine recombinase XerC
MLDISIQELIKQWQKYLILQKNYSNNTVIAYNNDLKHFLEFMNYYNSELVTLNHIKTADIRLIRSWLAKRKCENFTASSIARGLSTVKNFYKFLEKTLLLNNHIIFSIKSPKKAKLLPKGLSVDDVLISLEHIEEYGNVKWVELRNKALIVLIYAAGLRISEALSITKLHLQNLEFIKIIGKGSKERIIPWLPLTKNLITKYLEILPYKLDENEPIFRGRQGKKLQPSVFNRELIKLKRIYGLPEYLTAHSFRHSFASHLLEYGADLRSIQELLGHKSLSTTQKYTQTSIKHLEAVYNTAYPIKK
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids (By similarity).
Q9ZCE2
NTPP_RICPR
Nucleoside triphosphate pyrophosphatase (EC 3.6.1.9) (Nucleotide pyrophosphatase) (Nucleotide PPase)
MKQHIKNLPIILASGSLARVELLDRIKIIPTQIIPAYIDETPNLRELPAPLAIRLAYEKAIKVASQIETSSIIIAADTVTAVGRRILPKATTYEEVKHCIKMVSGRRHRVYTGLCIIKKENNQLTFRQKIVQTIIKFKKLSDEEINFYSSLDEGIDKAGGCKISGYAEAFVSFISGSYSNIMGLPLFETVNALTSLGFRYSNNTPNVYKDPSTNHLSKPSIS
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. {ECO:0000255|HAMAP-Rule:MF_00528}.
Q9ZCE3
IF1_RICPR
Translation initiation factor IF-1
MSKDDLIQFTGTVLELLPNATFRVKLENDHIIIAHTSGRMRKNRIRILLGDKVTVEMTPYDLTKGRVIHRH
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. {ECO:0000255|HAMAP-Rule:MF_00075}.
Q9ZCF2
ATPD_RICPR
ATP synthase subunit delta (ATP synthase F(1) sector subunit delta) (F-type ATPase subunit delta) (F-ATPase subunit delta)
MNKDNLIQNYAVALFNNALLDNIQVKICEEITLLNSIIEDSFEIKKFLFSPLVNKIDKINVFNSLVKTTNFNKIVNNFLLLLIKNSRTHILSNIVEVYNKLLYESRNIKIVHVISTNELQPKEQEWIQSRIEKELQHKTELFFDIDNTIIGGIVIKYDNVLRDYSIKGSLEKIAKCLKNVKIC
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-Rule:MF_01416}. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
Q9ZCF3
ATPE_RICPR
ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit)
MHETIRVKIITPSSIAFEKQSKMVTMPGEDGMFGVLPHHVPMIVNLKAGLVQIYIYNIHNYENTYLISGGVTEITSHYINIVTEVAINVTNLSESEISTQRYELQKLLSHQH
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q9ZCF7
NUOH_RICPR
NADH-quinone oxidoreductase subunit H (EC 7.1.1.-) (NADH dehydrogenase I subunit H) (NDH-1 subunit H)
MIEYFCEYMFPLTVIALKVVAITIPLILCVAYLTYAERRVIGLMQLRRGPNVVGPFGLLQPIADAVKLLFKEPIIPTDADKILFILAPIITFVLSLIGWAVIPFSSGVVLADINVGVLYILAISSLSVYGIIIAGWASNSKYAFLGAIRSSAQMISYEVSMGLVIITVLLTTGTLNLSGIIEAQKTLPWWIDLMLLPMSIVFFISVLAETNRLPFDLPEAESELVAGYNVEYSSMGFALFFLGEYANMILVSAMTTTLFLGGYLPPFNLSFLDCIPGFFWFVFKVGFLLFCFLWIRATLPRYRYDQLMRLGWKVFLPFTLFGVVLVSSVLFYTDNLPSV
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. {ECO:0000255|HAMAP-Rule:MF_01350}.
Q9ZCG0
NUOM_RICPR
NADH-quinone oxidoreductase subunit M (EC 7.1.1.-) (NADH dehydrogenase I subunit M) (NDH-1 subunit M)
MLELPIISITIFLPLISVLYILLFFNQNKKADKLSIYVAMLSSVLTFISTIYILIEFDVSNNTYQFVERYTWLDKIGLEFHVGVDGIAIFFVVLTSFLTLICIIGSLFTIKKYIKEYLVCFLLMESLCIGAFTSINLLLFYLFFEAILVPMYIIIGVWGGDNRIYAALKFFLYTFFGSVFFLLALIYIYSKIHSFDLTNILELIGNIPLFAQKILWWAIFIAFAIKTPMIPFHTWLPDAHVQAPTTGSVILAGILLKLGGYGFLRVLLPLFPNASQEFAIYVIYLSVIAIIYASLVALAQKDIKQMIAYSSIAHMGYVTIGIFSFTEIGISGAIFQMLSHGIISSSLFLIVGTLYERLHTKEIAKYGGVANKMPILATFFMIAMLSSIGLPSTSGFIGEFLSLLGIYKVNVVTAFIAALGIILGAVYMLKLYKEVMLGEITNTEIKHFRDLYKYEIISIAPLILLIIYFGLMPNSILNVFHLSVENLLIKF
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Q9ZCG1
NUOL_RICPR
NADH-quinone oxidoreductase subunit L (EC 7.1.1.-) (NADH dehydrogenase I subunit L) (NDH-1 subunit L)
MIHQNLAIMIIILPLVSSIINGLFLNIIDKKLAKIIAISFLSLSALFSLVIFCDVTLVGKIIHIKLLPWIEFKNLQVNWSIYIDQLTSIMFIAVTFVSSVVHIYSLGYMAEDKGIIRFLSFLSLFTFFMLMLVSADNFLQLFCGWEGVGVCSYLLIGFWHSKESANKAAIKAFITNRVSDFAFILGIITIIVYYGSANYKDVFSSAKLLSNTKIFVHFSILDIICLLLFIGCMGKSAQIGLHVWLPDAMEGPTPVSALIHAATMVTAGVFLVARCSYLFEYSPIVLQFITIIGGITCLFAASIAIMQSDIKKIIAYSTCSQLGYMFMACGVSSYNSAIFHLVTHAFFKALLFLSAGNVIHAVNEHNIFKMGGLINKMPITYGNFLIGSLALIGIYPLSGFYSKDLILEATYSSGSFMFIFGIITAILTAIYSMKIIILVFHGKTKLEKDVFKHAHEPTKIMNNPLILLVAGSFFSGMIGYYLLSMDKPNGYFHESLFNLHIYKLLINHHPLYIKLLPMAVGIVGIIIGICLYKGSLSYQTLTNESDQREKDWIPKSKCKMILVFISNVLRNKYYFDEIYNHLIIKPIHCLTYLFYFGDQKIIDRFGPNGFARVINYFCAVTCKIQTGYIFNYTLYIVSFIVVTISYFVLKNIY
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Q9ZCG3
NUOJ_RICPR
NADH-quinone oxidoreductase subunit J (EC 7.1.1.-) (NADH dehydrogenase I subunit J) (NDH-1 subunit J)
MPIFFYLFTTLIIISSLCVVLSKNSVYSVLWLIFTFINGSGLMILLGAEFLAMLLIVIYVGAVAVLFLFVIMMLDINFNQAITKLRENLSLSIFITLIMFADLVITIILSTKNINYSSNISFAIANNISNTKAIGNVLYTEFMLPFQIAGLILFVAMISCITLTLKKRDRIKHQDIRKQLSHNKSNVILMTKPILNKGVENIKYE
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Q9ZCG6
TATC_RICPR
Sec-independent protein translocase protein TatC
MKLYSFQEHLLEFKIRLLRIFTAFIIIFAICYYFSDYIYSFLLEPLAKLSGDTVRNIIYTGLTEAFFTYIKLSAFTAFTIIIPIIALECYLFISPGLYRHEKKIIAFILFMSPILFWCGSIFVFYFVMPKAWNFFLSFEKRDMIVPIILEARISEYLNLVIHLIIAFGIAFQLPIVIIVLNILKIVKTQTLKKKRRIAVVINFIIAGILTPPDILSQFALAIPLLLLYETSIIICNFIETPRTLNVKYQMD
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. {ECO:0000255|HAMAP-Rule:MF_00902}.
Q9ZCH7
KGUA_RICPR
Guanylate kinase (EC 2.7.4.8) (GMP kinase)
MKFKNKGLIIILSSPSGTGKSSLAKELLKIDNNLRLSISVTTRKPRLGEVDGINYYFKSDREFKTLVKQNKFLEYAKIYNDYYGTPKEYVKMLLKQGFDVLFDIDWQGVRSIKKNTNNVITIFILPPSIEILEQRLRNRATDNEETIKLRMQSAQNEISHANEYDYVVINDDFSQTLKKIHEIIVAERAKNFAYHEY
Essential for recycling GMP and indirectly, cGMP.
Q9ZCH9
ACP_RICPR
Acyl carrier protein (ACP)
MEFKIMSTTDKIEQKVIEMVAEKLNKDKAIITTDSRFIEDLKADSLDTVELMMAIEVEYGIDIPDDEATKIKTVSDVIKYIKERQS
Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}.
Q9ZCI9
RL21_RICPR
Large ribosomal subunit protein bL21 (50S ribosomal protein L21)
MFAVIKAGGKQYKVDRNSVIKVEKIDGELGSKIQFDQILMIGEYSKPSFIGTPIVKGAIVTAEITNQLKDNKIIAFKKKRRKNYRRKAGHRQELTELKILDITKQ
This protein binds to 23S rRNA in the presence of protein L20. {ECO:0000255|HAMAP-Rule:MF_01363}.
Q9ZCJ1
TATA_RICPR
Sec-independent protein translocase protein TatA
MGMSFSHLLIVLLIIFVLFGAGKLPQVMSDLAKGLKAFKEGMKDDGNDNDKTNN
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. {ECO:0000255|HAMAP-Rule:MF_00236}.
Q9ZCJ3
RSMI_RICPR
Ribosomal RNA small subunit methyltransferase I (EC 2.1.1.198) (16S rRNA 2'-O-ribose C1402 methyltransferase) (rRNA (cytidine-2'-O-)-methyltransferase RsmI)
MILKSGLYIVSTPIGNFEDITLRAISTLKNSDIILCEDTRISQKLLAKHYIHTKLQIYNDHSDYKDREYIISLIKAGNVVSLISDAGTPLISDPGYKLVRDLRNLNYYIEVVPGVSSPITALTLSSLPTDRFLFSGFLPKTIESKKKIFAELVNLKATLIFFDTASRLINTLLLAKEIFGNREICVARELTKIYQETKTGDIDEIIEFYKNNILKGEIVLLISGNVQVQNKQINLEKFIEFCLSKNLSSKTIIELAYDKFKDVYSKKEIYSVVHKKKFTA
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}.
Q9ZCL0
LPXK_RICPR
Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) (Lipid A 4'-kinase)
MIKLLYPQFWQERNIIAYLLLPISLIYQFLSYLRASLAYPVILPAQVICVGNCSVGGTGKTQIVIYLAKLLKAKNVPFVIITKAYGSHIKSTTIIQKGHTALEVGDEGIMLARYGTVIAAKYVKDILPLINELKPDVIIVDDFLQNPYLHKDFTIVSVDSQRLFGNRFLIPAGPLRQNPKQVLDAADLIFLVSSNQDQIPNELTPYIDKLINAQIVPSNNIDKNKNYFAFSGIGNPQRFFLTLENYRLNIVGYKIFPDHYNYLQADLENLYSLAKEHNAILITTRKDYVKFNYLNDEIICLDVELSINNPDLLNEKIFKKAKILN
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). {ECO:0000255|HAMAP-Rule:MF_00409}.
Q9ZCM4
LOLD_RICPR
Lipoprotein-releasing system ATP-binding protein LolD (EC 7.6.2.-)
MNNIVLILKMISKHYKQGNTIVRVLDGLNLTANEGELIAIIGSSGSGKSTLLHIAGLLDKPTNGQVIIPNIKYKKYHLIRLYYLGFIYQQHHLLKDFTALENVIIPRLIRGLDQKEAIKDATKILDDLGLEKKLYNMPGELSGGEQQRVAIARSLINKPRIILADEPTGNLDPNTTNEVFNLFLKVARKQNTTVIMVTHNHELAHKMDKLYNLKHGLLNIA
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01708}.
Q9ZCM8
Y696_RICPR
Putative export ATP-binding/permease protein RP696 (EC 7.-.-.-)
MDIKLLYRLAKYLRFYKKDLIIVMISLLSVSASLLLIGSIFRDLIDRGLAEDNILSVNKSILYICLLIVILSVASFFRSYFINNVAEKIVNQIRKEAYSNLINYEIEEYEELKIGDIISRLTNDIDQIATLIVNFLSFFIRNSVMLIGSITLMFFESFKLASIVIITIPILLVPLIKFGKHVKALSKKALESKSLLVSDIDETFNNIRVIYAFNHQINKIADFDTKLQSYLIYCKTRLKIRALFFAISIAVIFLTITLIVWIGASDIVQGDLSAGQIISFIYYAIIAGVSSGGIFELLSEMHLPTTALERIITIIDKTSIVHNNYYALNNSDAISIEFKNVDFTYNSRPNLKVINNMSLKINSNKFVGIVGRSGAGKSTLIQLLLRFYRQENGTILINNQDISFVKPTDIRKFIAYVPQEASIFSDTIKSNIIFGNNKASDYEINEIIKITGIEEFSTKLHDGINTKIGEKGVRLSGGQKQRIAIARALLRKPKILLLDEAMSALDTMSEQKLLNAIKKIMKGNIIISIAHRISSIESADYILVIDKGGVVTEGSHYDLSKNSEIYRNICREQLTI
Part of an ABC transporter complex. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).
Q9ZCN1
CLPX_RICPR
ATP-dependent Clp protease ATP-binding subunit ClpX
MVVDADKKELICSFCSKKQHEVKKLIAGPAVFICDECIDLCTDIMKEESKVALKQITASIPTPQKICKILNDYVVGQDQAKKILAVAVYNHYKRLEYVQSGNNDVELNKSNILLIGPTGSGKTLLAQTLAKILDVPFTMADATSLTEAGYVGEDVENILLRLLISAEFNIAKAQKGIIYIDEVDKIARKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQDFVQLDTSNILFICGGAFMGIDRIIRSRTNHSSIGFAANINIDKEKSNNEILKSLEIEDLTKFGLIPEFIGRLPIITTLDELDKEALITILTKPKNAIVKQYQKQFELDDADLVIDYSALEAIAEKALVKKTGARGLRSILEHLLLDSMYKVAELKKQRVTITKEVVDGLIEPCMTSIISTKLNKKQPIIEDIPA
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
Q9ZCN3
RMUC_RICPR
DNA recombination protein RmuC homolog
MPSLLLLTTTILLILCVLIIWFYIKTHTLKRQLQFLSEQNLEINNNNRLLNQEKIAYLQKIEQLKCKVEYQEQMIKDSEKIREESFTSAKAALFDLGKDLSKQLIEIHKIENNTARELAEQNITTASRKFNSELERLITMVGALNKDIEQSKSTVDLIKQSLLSPIGAGLLSEITLENILKSSGLRPNLDFIMQYGLTTSDSVKLRPDAIIFLPSGNLMVIDSKASKFLVDSQDNSVNLSKTMNYHLKSLANKDYAENILTTLNKKAHNFNNVITLMFLPTEQAVEKVIAANPEFLQKAWGCNIFPVGPAGLMNMLSFAKFQITDNRRSENYKVIISEVRKLLSSIGTIADYSKKIGYNLQNMVTNYDKFAASFNRNLMSRVKTIQKLGIDSGDKAMPATLERYQIVSSKSEIIEVDAENPTQIEE
Involved in DNA recombination.
Q9ZCN9
KTHY_RICPR
Thymidylate kinase (EC 2.7.4.9) (dTMP kinase)
MNKLTQGKFITFEGVDGIGKSTQSKMLYEYLKSQKIPVILTREVGGTTVAEKMREILVNEELLPMSELLQAMAARYDHMARKIIPALKDGYIVICDRFIDSTACYQGLELENGIDLVYSLHKTLMPSLMPDITFFIDVEPHTAIKRVNARNMSNKFDIRSIDFYKKIYTCFKELSNRFPERIKTIKASHLSPLEVHELIQKHL
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Q9ZCP6
DER_RICPR
GTPase Der (GTP-binding protein EngA)
MTKKIITLVGRPNVGKSTLFNRLSIRKKAIVHDLPGVTRDRKYTDGKIGSFEFLLIDTPGLEENPDNMGERLMGQTTQAILEADLICFMVDGKSGVLPDDKLLSNFVRKYNKHCILVVNKCEKAFDFDKEYYKLGFDSIVIISAEHGIGLIDLYDAIISKLSVEESIERNIADPFRGDCLQIVVSGRPNAGKSTFINAIINDERLLTGPEAGITRESIEVDWQYKNTHIKLIDTAGLRKKSTITASLEKLSTSDTINSIKFANTVILMIDALAHVKQQDFNIASHIVNEGRSIIIVVNKWDLVKESEKEAFQKEFYYQINTHLPQIKGVPVLFISAINKQNIEQVLDACLKIYKIWNKKITTNKLNKWLDFTTKIHPLPLQKCGRRVRIKYMTQIKTRPPTFKLFSNNPGKITDSYTRYLVNNMRDAFDMHGIPIRFTYVKNKNPYV
GTPase that plays an essential role in the late steps of ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
Q9ZCP8
EX7L_RICPR
Exodeoxyribonuclease 7 large subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII large subunit) (Exonuclease VII large subunit)
MIDNCIANQASKEFSVSEISNKIKELLENNFGYIKVKGEISGLKRASSGHAYFNLKENTAILACTCWRPILAKIKFPLNDGMEVVIGGKLSSYSGNSRYQLSVDNLQPAGLGAMLQILNERKTRLEKEGLFNKKRIPIPFLPDKIGVITSITGAVIKDIIHRIRERFPTRIIIWQVSVQGENSGHEMAEAIEGFNNLEEIHKPSVIIVARGGGSIEDLWSFNDEILVRAAYNSKIPIISAVGHEADYTLIDLAADKRAPTPTAAAEFAVPVRSILNNTIQSYEKILFNNTNRLIKYHEQSIVNYDKIHSYFSYYINNRQQLLDEIGFNLLDVLIRFIALKETKIKSFSKERINYAKIINYKILELTHQTAYLFKSVNNTLKNFEYKLELNSTLLASLDYHNVLKRGFAIVKGDAGNFLSSKSAATNEQSLNIKFFDGEINVVLSCHDLNTRSN
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
Q9ZCQ3
FTSZ_RICPR
Cell division protein FtsZ
MVLNIKAPENIVLKPTITVFGVGGAGSNAVNNMIHANLQGANFVVANTDAQSLEHSLCINKIQLGVSTTRGLGAGASPEVGALAAQESENEIRSSLENSNMVFITAGMGGGTGTGSAPIIARIAKELGILTVGVVTKPFHFEGGHRMKTADKGLIELQQFVDTLIVIPNQNLFRIANEQTTFADAFKMADDVLHAGVRGVTDLMIMPGLINLDFADIKAVMSEMGKAMMGTGEDSGEDRAIKAAESAISNPLLDHSSMCGARGVLINITGGPDMTLFEVDNAANRIREEVDNIDANIIFGSTFNPELKGIIRVSVVATGIDADKVPKYKLAIDKNTNTLPEETYNESIIQHTQIETIPSFNSYSTENIEINESSIKQDYTGNEQELRLHVNAVNKPENNSQKSSFLGKIWESLRTSNNQTLERKNVIVNTVDQDNKESDIHDIPAFLRKKRD
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}.
Q9ZCQ6
RL4_RICPR
Large ribosomal subunit protein uL4 (50S ribosomal protein L4)
MKTKILSLANEEVGEITLNKDIFAVEFIRDDIIKQVIDWQRAKAMFGNHKTKTVSEVSGTTKKPFKQKGTGNARQGSLRSVQMRGGGISHGPKVRSHAIKLPKKVRKLGLIHALSEKYAEEKLLIIDSLKLDKPKTSILVNLLSKFQGQSFFVIDGNKVDINFSLATKNIYNTLIVPQIGANVYDIIRHEYVLLSQEAVSFLEERLR
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of the polypeptide exit tunnel. {ECO:0000255|HAMAP-Rule:MF_01328}.
Q9ZCQ7
RL23_RICPR
Large ribosomal subunit protein uL23 (50S ribosomal protein L23)
MSVYKYYDLIRKPIITEKTTSISEQNKYTFYVNKFAKKLSLKRAIEAIFKVKVKKVNILNIKGKKKRFKGIIGTQINRKKAIVTLEKDHNIDYAGGIK
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
Q9ZCQ8
RL2_RICPR
Large ribosomal subunit protein uL2 (50S ribosomal protein L2)
MALKNFNPITPSLRELVQVDKTNLWKGRPLKTLTKGMSKTGGRNQQGRITSWHRGGGHKKLYRVIDFKRKKIDISAIVERIEYDPNRTAFIALIKYDDGEYSYILAPQKLSIGDRVISSQAADIKIGNCLPLKSIPIGTTLHNVEMKIGKGGQIARSAGTSVELVGKDSGYAQIKLRSGEFRLVPLDCKATIGSISNPDQKNINLGKAGRNRWLGWRPHVRGVAMNPVDHPHGGGEGKTSGGRHPVTPWGFSTKGKKTRKNKRTSKFIVKKRK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
Q9ZCQ9
RS19_RICPR
Small ribosomal subunit protein uS19 (30S ribosomal protein S19)
MARSIWKGPFVDGYLIKKVQKLMKSGKSEMIKTWSRRSTILPIFVGFTFSVHNGNKFIPVYINEEMVGRKLGEFAPTRTFHGHGADKKVKRK
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q9ZCR0
RL22_RICPR
Large ribosomal subunit protein uL22 (50S ribosomal protein L22)
MIQKNKNFATAKAKSIRVSPRKLNLVASFIRNMKVSEALVQLTFSPKRIAKIVKDCLQSAIANAENNLGLDIDRLIITKATVGKSVVMKRIMPRAKGRATRINKFFSNLYITVTEKEDN
This protein binds specifically to 23S rRNA its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
Q9ZCR1
RS3_RICPR
Small ribosomal subunit protein uS3 (30S ribosomal protein S3)
MGQKVCAHGFRVGPTLIKDWDSILYAEKHYKTLFIQDLKIRDLINKWFNQAQISRVLIERPSNKSIIININAKKPNIIIGKNGTEIDKLKKAIENMTFLKEVYINIHEVRKFNIDAAIVAQTIAAQLEKRVSFRKAMKTAIQASFKQGGQGIRVSCSGRLGGAEIARTEWYIEGRMPLHTLRADIDYSTAEAITTYGVIGVKVWIYKGEYKENKRYN
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-Rule:MF_01309}.
Q9ZCR2
RL16_RICPR
Large ribosomal subunit protein uL16 (50S ribosomal protein L16)
MLAPKKQKFRKAHKGRVMSKAKAGMTLAFGSFGLKSIDGWRVTARQIEAGRKAATRCMKRQGRLWIRIFPDVPVSKKPAEVRMGKGKGTPEFFAVRVSPGRIMFEIEGVEENIALRALELASAKLPVRTRIVRRYE
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
Q9ZCR4
RS17_RICPR
Small ribosomal subunit protein uS17 (30S ribosomal protein S17)
MPKRVLQGVVISSKTDKTVTVKVERKFKHPIYKKFVKVSKKYAAHDIENKYKEGDKVSIVESRPISKTKTWVVLNLE
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}.
Q9ZCR5
RL14_RICPR
Large ribosomal subunit protein uL14 (50S ribosomal protein L14)
MIQMQSILEVADNSGAKKVMCIKVLGGSHHMMAKLGDVIVVSIKEAIPGGKVKKGDVYKGVIVRTKTGVVRSDGSTIKFDKNALVLLNKQDEPIGTRVFGPVTRELRAKKYVRIMSLAEEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
Q9ZCR6
RL24_RICPR
Large ribosomal subunit protein uL24 (50S ribosomal protein L24)
MIKLKVKKGDEVVIITGKYKGKKGKVLKVFPEENTVVVSGVNLVKKHTKPNKMSEGGIITQESPIHISNIAHIDPKTGNPTKVAFKFLEDGSKVRVAKKSGEIIGKVGNNVKV
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
Q9ZCR7
RL5_RICPR
Large ribosomal subunit protein uL5 (50S ribosomal protein L5)
MLRFKELYKQKIIESLKKEFSFKNKHEIPKIKKIVINMGVGEAIADSKVINNALNDLTLISGQKPVVTLARKSIATFKLRENMKIGCKVTLRKDRMYDFLERLVIVALPRVKEFRGFSYKSFDGKGNFTFGLKEQIVFPEINYDKIDTIRGMDITIVTSAKTDQESKFLLSGFNLPFYN
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement. Contacts the P site tRNA the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}.
Q9ZCR8
RS14_RICPR
Small ribosomal subunit protein uS14 (30S ribosomal protein S14)
MAKVSSIQKNKSRQKKSQSLHNKRSELKSKIYDKSLSLEQRFPLIIALAQLPRNSSSTRIRNRCELTGRPRGVIRKFGISRNKLRELIGRGLVPGVVKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_00537}.
Q9ZCR9
RS8_RICPR
Small ribosomal subunit protein uS8 (30S ribosomal protein S8)
MSMTDNVADMLTRIRNAYKSKLINVSFPSSKIKTSILDVLQKEGYIKDYVTTQKNNISYTEVALKYSVNGEASICEIHRVSKPGKRVYSAIKDLKGYYNNMGIYILSTPYGVMSDREAHIKNVGGEVICKVF
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
Q9ZCS0
RL6_RICPR
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
MSRVGKLPITIPEGVKVGLNDLEVKISGPKGELSKTFKGNIAIIMEENKLVVKPLAVNKNARAMWGTARSIICNMITGVKEGFKLKLEINGVGYRAMVKGKYLNLMLAKSHNTKIEIPSNIKIDLPKQNIILLEGIDKEKLGQFASIIIKQRPPEPYKGKGIKFENKFIQRKEGKKN
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
Q9ZCS1
RL18_RICPR
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
MRSAKLKFEKRKSRIRYKISKTSNRMRLSIFKSCRHIYAQIIDDSKSITIAAASTLDKKIKKIKKSHCNIENAIKVGKEIAKKADSAGIKEVVFDRGGYKYHGIIKALADAAREKIKF
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}.