entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
P63265
|
CBPM_ECO57
|
Chaperone modulatory protein CbpM
|
MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPREIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP
|
Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}.
|
P63266
|
CBPM_SHIFL
|
Chaperone modulatory protein CbpM
|
MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPREIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP
|
Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}.
|
P64399
|
HRCA_MYCBO
|
Heat-inducible transcription repressor HrcA
|
MGSADERRFEVLRAIVADFVATQEPIGSKSLVERHNLGVSSATVRNDMAVLEAEGYITQPHTSSGRVPTEKGYREFVDRLEDVKPLSSAERRAIQSFLESGVDLDDVLRRAVRLLAQLTRQVAVVQYPTLSTSTVRHLEVIALTPARLLMVVITDSGRVDQRIVELGDVIDDHQLAQLREILGQALEGKKLSAASVAVADLASQLGGAGGLGDAVGRAATVLLESLVEHTEERLLLGGTANLTRNAADFGGSLRSILEALEEQVVVLRLLAAQQEAGKVTVRIGHETASEQMVGTSMVSTAYGTAHTVYGGMGVVGPTRMDYPGTIASVAAVALYIGDVLGAR
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
|
P64549
|
YFIR_ECO57
|
Protein YfiR
|
MRFSHRLFLLLILLLTGAPILAQEPSDVAKNVRMMVSGIVSYTRWPALSGPPKLCIFSSSRFSTALQENAATSLPYLPVIIHTQQEAMISGCNGFYFGNESPTFQMELTEQYPSKALLLIAEQNTECIIGSAFCLIIHNNDVRFAVNLDALSRSGVKVNPDVLMLARKKNDG
|
Repressor of the cell division arrest function of DgcN. Prevents DgcN relocation to the midcell.
|
P64635
|
HOFN_SHIFL
|
Putative DNA utilization protein HofN
|
MNPPINFLPWRQQRRTAFLRFWLLMFVAPLLLAVGITLILRLTGSAEARIDAVLLQAEQQLARSLQITKPRLLEQQQLREQRSQRQRQRQFTRDWQSALEALAALLPEHAWLTTISWQQGTLEIKGLTTSITALNALETSLRQDASFHLNQRGATQQDAQGRWQFEYQLTRKVSDEHVL
|
Required for the use of extracellular DNA as a nutrient.
|
P64910
|
MBCA_MYCBO
|
Mycobacterial cidal antitoxin MbcA
|
MGVNVLASTVSGAIERLGLTYEEVGDIVDASPRSVARWTAGQVVPQRLNKQRLIELAYVADALAEVLPRDQANVWMFSPNRLLEHRKPADLVRDGEYQRVLALIDAMAEGVFV
|
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the activity of cognate toxin MbcT by blocking access to the toxin active site.
|
P64942
|
PAFB_MYCBO
|
Protein PafB
|
MATSKVERLVNLVIALLSTRGYITAEKIRSSVAGYSDSPSVEAFSRMFERDKNELRDLGIPLEVGRVSALEPTEGYRINRDAYALSPVELTPDEAAAVAVATQLWESPELITATQGALLKLRAAGVDVDPLDTGAPVAIASAAAVSGLRGSEDVLGILLSAIDSGQVVQFSHRSSRAEPYTVRTVEPWGVVTEKGRWYLVGHDRDRDATRVFRLSRIGAQVTPIGPAGATTVPAGVDLRSIVAQKVTEVPTGEQATVWVAEGRATALRRAGRSAGPRQLGGRDGEVIELEIRSSDRLAREITGYGADAIVLQPGSLRDDVLARLRAQAGALA
|
Does not seem to be involved in pupylation or substrate degradation.
|
P64966
|
Y2292_MYCBO
|
Uncharacterized protein Mb2292c
|
MANDARPLARLANCRVGDQSSATHAYTVGPVLGVPPTGGVDLRYGGRAGIGRSETVTDHGAVGRRYHQPCAGQIRLSELRVTILLRCETLCETAQLLRCPPLPCDCSTPL
|
May play a regulatory role in sulfomenaquinone (SMK) biosynthesis.
|
P65016
|
ARYLT_MYCBO
|
Putative arylamide transporter
|
MSASLLVRTACGGRAVAQRLRTVLWPITQTSVVAGLAWYLTHDVFNHPQAFFAPISAVVCMSATNVLRARRAQQMIVGVALGIVLGAGVHALLGSGPIAMGVVVFIALSVAVLCARGLVAQGLMFINQAAVSAVLVLVFASNGSVVFERLFDALVGGGLAIVFSILLFPPDPVVMLCSARADVLAAVRDILAELVNTVSDPTSAPPDWPMAAADRLHQQLNGLIEVRANAAMVARRAPRRWGVRSTVRDLDQQAVYLALLVSSVLHLARTIAGPGGDKLPTPVHAVLTDLAAGTGLADADPTAANEHAAAARATASTLQSAACGSNEVVRADIVQACVTDLQRVIERPGPSGMSA
|
May be involved in the import of arylamide compounds.
|
P65068
|
YEFM_MYCBO
|
Antitoxin YefM
|
MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE
|
Antitoxin component of a type II toxin-antitoxin (TA) system. A probable antitoxin for the putative mRNA interferase YeoB (By similarity).
|
P65549
|
NRDI_MYCBO
|
Protein NrdI
|
MDIAGRSLVYFSSVSENTHRFVQKLGIPATRIPLHGRIEVDEPYVLILPTYGGGRANPGLDAGGYVPKQVIAFLNNDHNRAQLRGVIAAGNTNFGAEFCYAGDVVSRKCSVPYLYRFELMGTEDDVAAVRTGLAEFWKEQTCHQPSLQSL
|
Probably involved in ribonucleotide reductase function.
|
P65551
|
NRDI_STRP8
|
Protein NrdI
|
MAELIIVYFSSKSNNTHRFVQKLGLPAQRIPVDNRPLEVSTHYLLIVPTYAAGGSDAKGAVPKQVIRFLNNPNNRKHCKGVISSGNTNFGDTFALAGPIISQKLQVPLLHQFELLGTATDVKKVQAIFARLKHHTHDKQKQTNNLITERTHPCHKPMRHTSH
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
P67084
|
PLPHP_MYCBO
|
Pyridoxal phosphate homeostasis protein (PLP homeostasis protein)
|
MAADLSAYPDRESELTHALAAMRSRLAAAAEAAGRNVGEIELLPITKFFPATDVAILFRLGCRSVGESREQEASAKMAELNRLLAAAELGHSGGVHWHMVGRIQRNKAGSLARWAHTAHSVDSSRLVTALDRAVVAALAEHRRGERLRVYVQVSLDGDGSRGGVDSTTPGAVDRICAQVQESEGLELVGLMGIPPLDWDPDEAFDRLQSEHNRVRAMFPHAIGLSAGMSNDLEVAVKHGSTCVRVGTALLGPRRLRSP
|
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. {ECO:0000255|HAMAP-Rule:MF_02087}.
|
P67089
|
USPD_ECOL6
|
Universal stress protein D
|
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKLSADLLIVPFIDK
|
Required for resistance to DNA-damaging agents.
|
P67090
|
USPD_ECO57
|
Universal stress protein D
|
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKLSADLLIVPFIDK
|
Required for resistance to DNA-damaging agents.
|
P67248
|
Y1236_STAAM
|
UPF0122 protein SAV1236
|
MGQNDLVKTLRMNYLFDFYQSLLTNKQRNYLELFYLEDYSLSEIADTFNVSRQAVYDNIRRTGDLVEDYEKKLELYQKFEQRREIYDEMKQHLSNPEQIQRYIQQLEDLE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
P67249
|
Y1079_STAAN
|
UPF0122 protein SA1079
|
MGQNDLVKTLRMNYLFDFYQSLLTNKQRNYLELFYLEDYSLSEIADTFNVSRQAVYDNIRRTGDLVEDYEKKLELYQKFEQRREIYDEMKQHLSNPEQIQRYIQQLEDLE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
P67250
|
Y1119_STAAW
|
UPF0122 protein MW1119
|
MGQNDLVKTLRMNYLFDFYQSLLTNKQRNYLELFYLEDYSLSEIADTFNVSRQAVYDNIRRTGDLVEDYEKKLELYQKFEQRREIYDEMKQHLSNPEQIQRYIQQLEDLE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
P67251
|
Y1018_STRA3
|
UPF0122 protein gbs1018
|
MEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEESGVSRQAVYDNIKRTEKILEAYEMKLHMYSDYIVRSQIFDDILEKYTDDAFLQEKISILSSIDNRD
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
P67252
|
Y983_STRA5
|
UPF0122 protein SAG0983
|
MEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEESGVSRQAVYDNIKRTEKILEAYEMKLHMYSDYIVRSQIFDDILEKYTDDAFLQEKISILSSIDNRD
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
P67253
|
Y1201_STRP1
|
UPF0122 protein SPy_1201/M5005_Spy0916
|
MNIMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIADEFGVSRQAVYDNIKRTEKILETYEMKLHMYSDYVVRSEIFDDMIAHYPHDEYLQEKISILTSIDNRE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein (By similarity).
|
P67255
|
Y1152_STRP8
|
UPF0122 protein spyM18_1152
|
MNIMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIADEFGVSRQAVYDNIKRTEKILETYEMKLHMYSDYVVRSEIFDDMIAHYPHDEYLQEKISILTSIDNRE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein (By similarity).
|
P67299
|
PARD_MYCBO
|
Antitoxin ParD
|
MGKNTSFVLDEHYSAFIDGEIAAGRYRSASEVIRSALRLLEDRETQLRALREALEAGERSGSSTPFDFDGFLGRKRADASRGR
|
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of toxin ParE (By similarity).
|
P67302
|
YIDD_NEIMA
|
Putative membrane protein insertion efficiency factor
|
MNFLLSKLLLGLIRFYQYCISPLIPPRCRYTPTCSQYAVEAVKKYGAFKGGRLAIKRIARCHPFGGHGHDPVP
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67303
|
YIDD_NEIMB
|
Putative membrane protein insertion efficiency factor
|
MNFLLSKLLLGLIRFYQYCISPLIPPRCRYTPTCSQYAVEAVKKYGAFKGGRLAIKRIARCHPFGGHGHDPVP
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67304
|
YIDD_STAAM
|
Putative membrane protein insertion efficiency factor
|
MKKIFLAMIHFYQRFISPLTPPTCRFYPTCSEYTREAIQYHGAFKGLYLGIRRILKCHPLHKGGFDPVPLKKDKSASKHSHKHNH
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67305
|
YIDD_STAAN
|
Putative membrane protein insertion efficiency factor
|
MKKIFLAMIHFYQRFISPLTPPTCRFYPTCSEYTREAIQYHGAFKGLYLGIRRILKCHPLHKGGFDPVPLKKDKSASKHSHKHNH
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67306
|
YIDD_STAAW
|
Putative membrane protein insertion efficiency factor
|
MKKIFLAMIHFYQRFISPLTPPTCRFYPTCSEYTREAIQYHGAFKGLYLGIRRILKCHPLHKGGFDPVPLKKDKSASKHSHKHNH
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67307
|
YIDD_STRP1
|
Putative membrane protein insertion efficiency factor
|
MKKLLIVSVKAYQKYISPLSPPSCRYKPTCSAYMLTAIEKHGTKGILMGIARILRCHPFVAGGVDPVPEDFSLMRNKNTSKNAEKA
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P67369
|
Y2440_MYCBO
|
DegV domain-containing protein Mb2440c
|
MTVVVVTDTSCRLPADLREQWSIRQVPLHILLDGLDLRDGVDEIPDDIHKRHATTAGATPVELSAAYQRALADSGGDGVVAVHISSALSGTFRAAELTAAELGPAVRVIDSRSAAMGVGFAALAAGRAAAAGDELDTVARAAAAAVSRIHAFVAVARLDNLRRSGRISGAKAWLGTALALKPLLSVDDGKLVLVQRVRTVSNATAVMIDRVCQLVGDRPAALAVHHVADPAAANDVAAALAERLPACEPAMVTAMGPVLALHVGAGAVGVCVDVGASPPA
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67370
|
Y1425_STAAM
|
DegV domain-containing protein SAV1425
|
MTKQIIVTDSTSDLSKEYLEANNIHVIPLSLTIEGASYVDQVDITSEEFINHIENDEDVKTSQPAIGEFISAYEELGKDGSEIISIHLSSGLSGTYNTAYQASQMVDANVTVIDSKSISFSLGYQIQHLVELVKEGVSTSEIVKKLNHLRENIKLFVVIGQLNQLIKGGRISKTKGLIGNLMKIKPIGTLDDGRLELVHNARTQNSSIQYLKKEIAEFIGDHEIKSIGVAHANVIEYVDKLKKVFNEAFHVNNYDINVTTPVISAHTGQGAIGLVVLKK
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67371
|
Y1258_STAAN
|
DegV domain-containing protein SA1258
|
MTKQIIVTDSTSDLSKEYLEANNIHVIPLSLTIEGASYVDQVDITSEEFINHIENDEDVKTSQPAIGEFISAYEELGKDGSEIISIHLSSGLSGTYNTAYQASQMVDANVTVIDSKSISFSLGYQIQHLVELVKEGVSTSEIVKKLNHLRENIKLFVVIGQLNQLIKGGRISKTKGLIGNLMKIKPIGTLDDGRLELVHNARTQNSSIQYLKKEIAEFIGDHEIKSIGVAHANVIEYVDKLKKVFNEAFHVNNYDINVTTPVISAHTGQGAIGLVVLKK
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67373
|
Y1511_STRP8
|
DegV domain-containing protein spyM18_1511
|
MGTIKIVTDSSITIEPELIKALDITVVPLSVMIDSKLYSDNDLKEEGHFLSLMKASKSLPKTSQPPVGLFAETYENLVKKGVTDIVAIHLSPALSGTIEASRQGAEIAEAPVTVLDSGFTDQAMKFQVVEAAKMAKAGASLNEILAAVQAIKSKTELYIGVSTLENLVKGGRIGRVTGVLSSLLNVKVVMALKNDELKTLVKGRGNKTFTKWLDSYLAKNSHRPIAEIAISYAGEASLALTLKERIAAYYNHSISVLETGSIIQTHTGEGAFAVMVRYE
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67374
|
Y1936_STRP1
|
DegV domain-containing protein SPy_1936/M5005_Spy1650
|
MTFTIMTDSTADLNQTWAEDHDIVLIGLTILCDGEVYETVGPNRISSDYLLKKMKAGSHPQTSQINVGEFEKVFREHARNNKALLYLAFSSVLSGTYQSALMARDLVREDYPDAVIEIVDTLAAAGGEGYLTILAAEARDSGKNLLETKDIVEAVIPRLRTYFLVDDLFHLMRGGRLSKGSAFLGSLASIKPLLWIDEEGKLVPIAKIRGRQKAIKEMVAQVEKDIADSTVIVSYTSDQGSAEKLREELLAHENISDVLMMPLGPVISAHVGPNTLAVFVIGQNSR
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67375
|
Y2003_STRP8
|
DegV domain-containing protein spyM18_2003
|
MTFTIMTDSTADLNQTWAEDHDIVLIGLTILCDGEVYETVGPNRISSDYLLKKMKAGSHPQTSQINVGEFEKVFREHARNNKALLYLAFSSVLSGTYQSALMARDLVREDYPDAVIEIVDTLAAAGGEGYLTILAAEARDSGKNLLETKDIVEAVIPRLRTYFLVDDLFHLMRGGRLSKGSAFLGSLASIKPLLWIDEEGKLVPIAKIRGRQKAIKEMVAQVEKDIADSTVIVSYTSDQGSAEKLREELLAHENISDVLMMPLGPVISAHVGPNTLAVFVIGQNSR
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P67615
|
FETP_NEIMA
|
Probable Fe(2+)-trafficking protein
|
MARMVFCVKLNKEAEGMKFPPLPNELGKRIFENVSQEAWAAWTRHQTMLINENRLSLADPRAREYLAQQMEQYFFGDGADAVQGYVPQ
|
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}.
|
P68550
|
VH21_MYXVL
|
Probable host range protein 2-1
|
MGVQHKLDIFLVSEGIAIKEANLLKGDSYGCTIKIKLDKEKTFKFVIVLEPEWIDEIKPIYMKVNDESVELELDYKDAIKRIYSAEVVLCSDSVINLFSDVDVSYTCEYPTIKVNTIKKYYSVQNRGMTYVHIESPINTKDKCWFVEKNGWYEDRTHS
|
Plays a role for multiplication of the virus in different cell types.
|
P68552
|
VH21_MYXVU
|
Probable host range protein 2-1
|
MGVQHKLDIFLVSEGIAIKEANLLKGDSYGCTIKIKLDKEKTFKFVIVLEPEWIDEIKPIYMKVNDESVELELDYKDAIKRIYSAEVVLCSDSVINLFSDVDVSYTCEYPTIKVNTIKKYYSVQNRGMTYVHIESPINTKDKCWFVEKNGWYEDRTHS
|
Plays a role for multiplication of the virus in different cell types.
|
P68642
|
PG027_CAMPS
|
Interferon antagonist OPG027 (Host range protein 2)
|
MGIQHEFDIIINGDIALRNLQLHRGDNYGCKLKIISNDYKKLKFRFIIRPDWSEIDEVKGLTVFANNYVVKVNKVDDTFYYVIYEAVIHLYNKKTEILIYSDDEKELFKHYYPYISLNMISKKYKVKEENYSSPYIEHPLIPYRDYESMD
|
Inhibits antiviral activity induced by type I interferons. Does not block signal transduction of IFN, but is important to counteract the host antiviral state induced by a pre-treatment with IFN (By similarity).
|
P68643
|
PG027_CAMPM
|
Probable host range protein 2
|
MGIQHEFDIIINGDIALRNLQLHRGDNYGCKLKIISNDYKKLKFRFIIRPDWSEIDEVKGLTVFANNYVVKVNKVDDTFYYVIYEAVIHLYNKKTEILIYSDDEKELFKHYYPYISLNMISKKYKVKEENYSSPYIEHPLIPYRDYESMD
|
Inhibits antiviral activity induced by type I interferons. Does not block signal transduction of IFN, but is important to counteract the host antiviral state induced by a pre-treatment with IFN (By similarity).
|
P68647
|
FIXX_ECOL6
|
Ferredoxin-like protein FixX
|
MTSPVNVDVKLGVNKFNVDEEHPHIVVKADADKQALELLVKACPAGLYKKQDDGSVRFDYAGCLECGTCRILGLGSALEQWEYPRGTFGVEFRYG
|
Could be part of an electron transfer system required for anaerobic carnitine reduction. Could be a 3Fe-4S cluster-containing protein (By similarity).
|
P68648
|
FIXX_ECO57
|
Ferredoxin-like protein FixX
|
MTSPVNVDVKLGVNKFNVDEEHPHIVVKADADKQALELLVKACPAGLYKKQDDGSVRFDYAGCLECGTCRILGLGSALEQWEYPRGTFGVEFRYG
|
Could be part of an electron transfer system required for anaerobic carnitine reduction. Could be a 3Fe-4S cluster-containing protein (By similarity).
|
P68657
|
EA10_ECOL6
|
Lambda prophage-derived protein ea10
|
MSNIKKYIIDYDWKASIEIEIDHDVMTEEKLHQINNFWSDSEYRLNKHGSVLNAVLIMLAQHALLIAISSDLNAYGVVCEFDWNDGNGQEGWPPMDGSEGIRITDIDTSGIFDSDDMTIKAA
|
The ea10 gene protein is believed to be involved in the production of the Tro phenotype. This phenotype is expressed when phages that possess a mutant cro gene and a thermolabile cI repressor gene are unable to propagate at restrictive temperatures. This inability is correlated with the shutoff of host macromolecular synthesis (By similarity).
|
P68658
|
EA10_LAMBD
|
Protein ea10
|
MSNIKKYIIDYDWKASIEIEIDHDVMTEEKLHQINNFWSDSEYRLNKHGSVLNAVLIMLAQHALLIAISSDLNAYGVVCEFDWNDGNGQEGWPPMDGSEGIRITDIDTSGIFDSDDMTIKAA
|
The ea10 gene protein is believed to be involved in the production of the Tro phenotype. This phenotype is expressed when phages that possess a mutant cro gene and a thermolabile cI repressor gene are unable to propagate at restrictive temperatures. This inability is correlated with the shutoff of host macromolecular synthesis.
|
P68659
|
VHTJ_ECOL6
|
Lambda prophage-derived head-to-tail joining protein W (gpW)
|
MTRQEELAAARAALHDLMTGKRVATVQKDGRRVEFTATSVSDLKKYIAELEVQTGMTQRRRGPAGFYV
|
Required for the stabilization of DNA within the phage head and for attachment of tails onto the head during morphogenesis.
|
P68709
|
A20_VACCA
|
DNA polymerase processivity factor component A20
|
MTSSADLTNLKELLSLYKSLKFSDSAAIEKYNSLVEWGTSTYWKIGVQKVANVETSISDYYDEVKNKPFNIDPGYYIFLPVYFGSVFIYSKGKNMVELGSGNSFQIPDDMRSACNKVLDSDNGIDFLRFVLLNNRWIMEDAISKYQSPVNIFKLASEYGLNIPKYLEIEIEEDTLFDDELYSIIERSFDDKFPKISISYIKLGELRRQVVDFFKFSFMYIESIKVDRIGDNIFIPSVITKSGKKILVKDVDHLIRSKVREHTFVKVKKKNTFSILYDYDGNGTETRGEVIKRIIDTIGRDYYVNGKYFSKVGSAGLKQLTNKLDINECATVDELVDEINKSGTVKRKIKNQSAFDLSRECLGYPEADFITLVNNMRFKIENCKVVNFNIENTNCLNNPSIETIYGNFNQFVSIFNIVTDVKKRLFE
|
Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity).
|
P68730
|
DEGR_BACNA
|
Regulatory protein DegR
|
MDDKDLKLILHKTFIEIYSDLEELADIAKKGKPSMEKYVEEIEQRCKQNILAIEIQMKIK
|
Stabilizes the phosphorylated form of DegU, leading to enhanced production of levansucrase, alkaline protease, and neutral protease.
|
P68811
|
NRDI_STAAM
|
Protein NrdI
|
MKIIYFSFTGNVRRFIKRTELENTLEITAENCMEPVHEPFIIVTGTIGFGEVPEPVQSFLEVNHQYIRGVAASGNRNWGLNFAKAGRTISEEYNVPLLMKFELHGKNKDVIEFKNKVGNFNENHGREKVQSY
|
Probably involved in ribonucleotide reductase function.
|
P68812
|
NRDI_STAAN
|
Protein NrdI
|
MKIIYFSFTGNVRRFIKRTELENTLEITAENCMEPVHEPFIIVTGTIGFGEVPEPVQSFLEVNHQYIRGVAASGNRNWGLNFAKAGRTISEEYNVPLLMKFELHGKNKDVIEFKNKVGNFNENHGREKVQSY
|
Probably involved in ribonucleotide reductase function.
|
P68814
|
NRDI_STAAW
|
Protein NrdI
|
MKIIYFSFTGNVRRFIKRTELENTLEITAENCMEPVHEPFIIVTGTIGFGEVPEPVQSFLEVNHQYIRGVAASGNRNWGLNFAKAGRTISEEYNVPLLMKFELHGKNKDVIEFKNKVGNFNENHGREKVQSY
|
Probably involved in ribonucleotide reductase function.
|
P68879
|
IPGE_SHISO
|
Chaperone protein IpgE
|
MEDLADVICRALGIPLIDIDDQAIMLDDDVLIYIEKEGDSINLLCPFCALPENINDLIYALSLNYSEKICLATDDEGGNLIARLDLTGINEFEDVYVNTEYYISRVRWLKDEFARRMKGY
|
Molecular chaperone required for IpgD stabilization and secretion.
|
P68924
|
REXA_LAMBD
|
Protein rexA
|
MKNGFYATYRSKNKGKDKRSINLSVFLNSLLADNHHLQVGSNYLYIHKIDGKTFLFTKTNDKSLVQKINRSKASVEDIKNSLADDESLGFPSFLFVEGDTIGFARTVFGPTTSDLTDFLIGKGMSLSSGERVQIEPLMRGTTKDDVMHMHFIGRTTVKVEAKLPVFGDILKVLGATDIEGELFDSLDIVIKPKFKRDIKKVAKDIIFNPSPQFSDISLRAKDEAGDILTEHYLSEKGHLSAPLNKVTNAEIAEEMAYCYARMKSDILECFKRQVGKVKD
|
May confer an overall protective ability to the host cell by triggering a growth arrest and avoiding lethal host gene expression. Additionally, may confer symbiotic protection to the lysogenic host against secondary infection.
|
P68925
|
REXA_BP434
|
Protein rexA
|
MKNGFYATYRSKNKGKDKRSINLSVFLNSLLADNHHLQVGSNYLYIHKIDGKTFLFTKTNDKSLVQKINRSKASVEDIKNSLADDESLGFPSFLFVEGDTIGFARTVFGPTTSDLTDFLIGKGMSLSSGERVQIEPLMRGTTKDDVMHMHFIGRTTVKVEAKLPVFGDILKVLGATDIEGELFDSLDIVIKPKFKRDIKKVAKDIIFNPSPQFSDISLRAKDEAGDILTEHYLSEKGHLSAPLNKVTNAEIAEEMAYCYARMKSDILECFKRQVGKVKD
|
Inhibits the growth of unrelated coliphages, including T4rII, T5lr, T1, and some mutants of T7, P22, phi-80, and lambda. It controls the activity of gene S and may inhibit the establishment of lysogeny by the repressor protein (By similarity).
|
P69173
|
VGC_BPS13
|
C protein
|
MRKFDLSLRSSRSSYFATFRHQLTILSKTDALDEEKWLNMLGTFVKDWFRYESHFVHGRDSLVDILKERGLLSESDAVQPLIGKKS
|
C protein is one of the proteins involved in the production and packaging of viral single-stranded DNA.
|
P69189
|
NDD_BPT2
|
Nucleoid disruption protein (Nuclear disruption protein)
|
MKYMTVTDLNNAGATVIGTIKGGEWFLGTPHKDILSKPGFYFLVSKLDGRPFSNPCVSARFYVGNQRSKQGFSAVLSHIRQRRSQLARTIANNNVPYTVFYLPASKMKPLTTGFGKGQLALAFTRNHHSEYQTLEEMNRMLADNFKFVLQAY
|
Disorganizes the host nucleoid and inhibits replication, but without host DNA cleavage or degradation. Only the architecture of the nucleoid is affected. May act on the host chromosomal sequences that determine the structure of the nucleoid. Binds to dsDNA but not to ssDNA.
|
P69190
|
NDD_BPR32
|
Nucleoid disruption protein (Nuclear disruption protein)
|
MKYMTVTDLNNAGATVIGTIKGGEWFLGTPHKDILSKPGFYFLVSKLDGRPFSNPCVSARFYVGNQRSKQGFSAVLSHIRQRRSQLARTIANNNVPYTVFYLPASKMKPLTTGFGKGQLALAFTRNHHSEYQTLEEMNRMLADNFKFVLQAY
|
Disorganizes the host nucleoid and inhibits replication, but without host DNA cleavage or degradation. Only the architecture of the nucleoid is affected. May act on the host chromosomal sequences that determine the structure of the nucleoid. Binds to dsDNA but not to ssDNA.
|
P69191
|
NDD_BPK3
|
Nucleoid disruption protein (Nuclear disruption protein)
|
MKYMTVTDLNNAGATVIGTIKGGEWFLGTPHKDILSKPGFYFLVSKLDGRPFSNPCVSARFYVGNQRSKQGFSAVLSHIRQRRSQLARTIANNNVPYTVFYLPASKMKPLTTGFGKGQLALAFTRNHHSEYQTLEEMNRMLADNFKFVLQAY
|
Disorganizes the host nucleoid and inhibits replication, but without host DNA cleavage or degradation. Only the architecture of the nucleoid is affected. May act on the host chromosomal sequences that determine the structure of the nucleoid. Binds to dsDNA but not to ssDNA.
|
P69203
|
RPC2_BPP21
|
Repressor protein C2
|
MNTQL
|
This protein allows the phage to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein C2 to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
|
P69595
|
VGK_BPS13
|
K protein
|
MSRKIILIKQELLLLVYELNRSGLLAENEKIRPILAQLEKLLLCDLSPSTNDSVKN
|
No function has yet been ascribed to K protein.
|
P69626
|
REGA_BPT6
|
Translation repressor protein
|
MIEITLKKPEDFLKVKETLTRMGIANNKDKVLYQSCHILQKKGLYYIVHFKEMLRMDGRQVEMTEEDEVRRDSIAWLLEDWGLIEIVPGQRTFMKDLTNNFRVISFKQKHEWKLVPKYTIGN
|
Controls the translation of a number of proteins (such as regA itself, rIIB and at least 35 others) by binding to their mRNA.
|
P69627
|
REGA_BPR18
|
Translation repressor protein
|
MIEITLKKPEDFLKVKETLTRMGIANNKDKVLYQSCHILQKKGLYYIVHFKEMLRMDGRQVEMTEEDEVRRDSIAWLLEDWGLIEIVPGQRTFMKDLTNNFRVISFKQKHEWKLVPKYTIGN
|
Controls the translation of a number of proteins (such as regA itself, rIIB and at least 35 others) by binding to their mRNA.
|
P69628
|
REGA_BPR51
|
Translation repressor protein
|
MIEITLKKPEDFLKVKETLTRMGIANNKDKVLYQSCHILQKKGLYYIVHFKEMLRMDGRQVEMTEEDEVRRDSIAWLLEDWGLIEIVPGQRTFMKDLTNNFRVISFKQKHEWKLVPKYTIGN
|
Controls the translation of a number of proteins (such as regA itself, rIIB and at least 35 others) by binding to their mRNA.
|
P69701
|
REGA_BPT2
|
Translation repressor protein
|
MIEITLKKPEDFLKVKETLTRMGIANNKDKVLYQSCHILQKKGLYYIVHFKEMLRMDGRQVEMTEEDEVRRDSIAWLLEDWGLIEIVPGQRTFMKDLTNNFRVISFKQKHEWKLVPKYTIGN
|
Controls the translation of a number of proteins (such as regA itself, rIIB and at least 35 others) by binding to their mRNA.
|
P69960
|
LCRR_YERPS
|
Low calcium response locus protein R
|
MMADPLIPWLTEHGLVCHPHTLSGTPISLGSAFQLAGLKLAWRVEIEQRRVWIVLIQRVEQRRGLKNPFAALYMLANAARAVLGPDYYLYGNVDVLAGSSLSTQRLAHFYRRWTGAKELSTGWFSLKVSQVITLSNMKKRQNNGFA
|
Involved in the down-regulation of lcrGVH transcription in the presence or absence of calcium and is necessary for lcrG protein expression in the absence of calcium. Plays an important role in the regulation of the low-calcium response.
|
P70742
|
DSRD_ARCFU
|
Protein DsrD
|
MADYTEEDKQKVLAQLSKKTWKIPELAKILKMDKKVVKKIVQDLINEGVAGYWSSGSTTYVATKEYIEELEKKRAEG
|
May play an essential role in dissimilatory sulfite reduction.
|
P70949
|
SUFT_BACSU
|
Fe-S protein maturation auxiliary factor YitW (Iron-sulfur cluster assembly factor YitW)
|
MEEALKENIMGALEQVVDPELGVDIVNLGLVYDVDMDEDGLTHITMTLTSMGCPLAPIIVDEVKKALADLPEVKDTEVHIVWNPPWTRDKMSRYAKIALGIQ
|
Involved in the maturation of iron-sulfur (Fe-S) proteins. May function as a Fe-S cluster carrier.
|
P71344
|
T1SI_HAEIN
|
Putative type I restriction enzyme specificity subunit S.HindORF215P (S protein) (S.HindORF215P)
|
MKNNRTFLEKLLEGSEVEWKPLDEVANIVNNARKPVKSSLRVSGNIPYYGANNIQDYVEGYTHEGEFVLIAEDGSASLENYSIQWAVGKFWANNHVHVVNGKEKLNNRFLYHYLTNMNFIPFLAGKERAKLTKAKLQQIPIPIPPLSVQTEIVKILDALTALTSELTSELTSELTSELILRQKQYEYYREKLLNIDEMNKVIELGDVGPVRMCKRILKNQTASSGDIPFYKIGTFGKKPDAYISNELFQEYKQKYSYPKKGDILISASGTIGRTVIFDGENSYFQDSNIVWIDNDETLVLNKYLYHFYKIAKWGIAEGGTIQRLYNDNLKKVKISIPPLKEQHRIVSILDKFETLTNSITEGLPLAIEQSQKRYEYYRELLLNFS
|
A putative specificity subunit for a type I restriction enzyme the corresponding endonuclease and methylase subunits have multiple frameshifts and are probably not expressed.
|
P71388
|
VPC_HAEIN
|
Mu-like prophage FluMu protein C
|
MAHYFGGKSFYLPAGDKIKEALRDAQIYQEFNGKNVPDLIKKYRLSESTIYAILRNQRTLQRKRHQMDFNFS
|
Required for transcription of the phage late genes.
|
P71498
|
HRCA_MYCCT
|
Heat-inducible transcription repressor HrcA
|
MLTKRQVKILQTIVEEFIKTNQPVGSKRILELLDIKISSATIRNESAILEHEGYLEKQHTSSGRTPSTKGYRYYVDNIMKLDSADYTRLKIYLNQLLDLRKYDIDKTINYASEIISELTKMTAVVIKKQNIKNIKLKKIELILLSEFLASVLFIFSDGDVQNKMFNLKDISLSDLKIAIKLFSDFLVDVKLDEIDQYLNDLKHQLSLSIKQYDYVLNTFINTILESKNEQKETHGMRYMLENPEFNDTNKLKNAVKLVEQLSPFDWFNIAYESNKNMNKIAIKIGNEIDQINDDISMIATELKIGNSSTVLTLVGPKRVDYNQVNQLMNLIIEIINAKEN
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
|
P73345
|
SMF_SYNY3
|
Protein Smf
|
MANSEQAYWLAWSQVKGVGPVLLKRLAQHFELLENAWKARPIALGEVEGFGHKMIEKIIGQRNNLNPFQFLEEHQQKNPQFLTPDDPDYPRLLWEIPSPPPVLYYLGRLDHRESQGQIPGVGIVGTRYPTDHGSRWTRKISQALVKSGFTIVSGLAAGIDADAHSSCLRVNGRTIAVLGTGLDLIYPPQNRQLFEQIAAEGLILSEYPVGSKPERGNFPARNRIIAGLSRAVLVMEAPPKSGALITAKYANEFNRDVFSLPNSPDVQEAHGCLNLIHNGAEVILSENQLLASLGAIPLLDQGQEQKILPGDRQIGYLDQTNVPTLTTGARGKQPLTEPPEDLEPTLKKILAAVQEEPTALDQIVAVTALAIGDVSAGLLQLEILGLVSQEPGMRYQRR
|
May help load RecA onto ssDNA (By similarity).
|
P73720
|
OPCA_SYNY3
|
Putative OxPP cycle protein OpcA
|
MGGKYQRHCPVRFHWSHCMSTTQAPPLVSLQAPKDVSLEAIESELAQIWQTSAQKEEGLIATRATTFSFLVYEPDRVQSLLAALGYYTGPIDGITGPRMTAAIKSAQKALGVTATGLSSPEFKQALQTAFETAHREGNLLSTAERITKPYSPDLEGSGIADTIAASNPCRIITLCPTAEDDQGVQAQLSAYCPIQKTHQNTLICCEYITLRGTSDALERIGGVITELMLPTLPKYVWWKASPEAEYGLFQRLLSHADMIIVDSSIFNNPEQDLLQLAQLVNKPEAIADLNWSRLAPWQELTAEAFDPPERRSAVGEIDQISIDYEKGNHAQALMYLGWVASRLQWTPVSYSYQPGVYEIHKIQFCAPNQRPIEAELAGLPLADTGQVLGDLISLKLGSTNTQAQCGTVLCSGTVGCMRMEAGGGAQNYRVQQVTALDDQNTEQLLGRQLQRWGRDALYDESMAIVLAILQLSQAG
|
May be involved in the functional assembly of glucose 6-phosphate dehydrogenase.
|
P75312
|
Y472_MYCPN
|
DegV domain-containing protein MG326 homolog
|
MKTAIITDSTASIKEGEIQDVYVLPLQVIINGQDTYRDGKDIDYDRVYQLLKEHPQGLNISTSLPRQADLIELIEAIKDKYDRFVFLPLSKGLSGTYDMIVQAVKPLSTPKKEFVVLETSDIAISLKWLVQEVKALTDTNCPTKAIAEVVDQHKQSIFTAVTVKNLVQLRKGGRISGLKKIIATLLRVKPIIFFDKGVNTLSGKAFTFVQALEKIFTFVKSKFGDNFKIKRIGFCNAFTPVKAKEVKALILDFLHTNKITLQREIESSFITSAIIAHTGIDAFSISLLLDKNK
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
P75363
|
Y424_MYCPN
|
UPF0122 protein MPN_424
|
MNQTKLNQRLKQQQLFDIYGELLTKRQACYFNEYINLDLSMQEIADKYQVKKSSIHQHIKTCNLIFNRFEAKLQLFKKQQLRLKLYEKITDPQLREQLIKLR
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein (By similarity).
|
P75432
|
T1R2_MYCPN
|
Putative type I restriction enzyme MpnIIP endonuclease subunit middle part (R protein middle part)
|
MSDALDDENVLCFRYKSYYIKDDGSRIDTLNEERIKHIVDFTLDKYLDATQNTPKFDNFENPVKEGFNSIFACESKEAAIEYYKEFKKQIEQKKLPIKIASIIAQTKVVMNKKLV
|
The middle section of a putative type I restriction enzyme that if reconstituted might recognize 5'-GAN(7)TAY-3' and cleave a random distance away (Probable). Subunit R is required for both nuclease and ATPase activities, but not for modification.
|
P75452
|
TRRMC_MYCPN
|
Putative type II restriction enzyme and methyltransferase RM.MpnORF110P C-terminus
|
MKIRISLNILAKFLDSFAHLLFLKNKEIYTPRKEQAACVEVLERYFQANPENGRFLMNCKMRFGKCFTLYSYAQKNNINKILILTFVPAVEESLKDDLNHIEKNYKFYTDDDLQKSNFDLKNQNEPYVVFLSLQNVLGKQRIDGAKTDFDKERISKLQEIDFDLIVFDEYHYGANKKRTQIKVEKVNKKIDNPEQQDNQDDAEEELASTFKLKDIKSKFQFSYKQLVCLSGTPFSSLRNNEFSSKDQVFTYSYFDEQKAKSAENHPLKLGQYGIFPEMNIYCFELAEIFTAQEQEIFITPGKGKNKLPEISFRKLFQTENVSKESSKPVYRFVNENLVEKLIDSLIDKRKGFSHTPLSWENIDKHKHSLLILPTRVACFALANLLKNHWYFENNDFQIINMSESQFGNGKKALIELNKHLDEAKKTNKNTLTITVAKLTIGITVKEWSTVFFLKDLKGAESYFQTIFRIQTPYIKNCKNLKEICYVYDFNMYRCLEVTNEYSKQTQTDPKFSASWFQNLDKFLPIYLVRGDEIQKTDPEILQKYEYFIMDKRAFSTRWMDESNIIDIDVLCNVGQDEDAQKILKKILAHKKFKSSKKKREFEDVHLEKSPKSEAFSEGVRSGKDYAAEQGNVLEELENFWNFNQALEQKAKAEFQQKNFDDNEWNNYKKGFNFGVNKHFEDKVSIKKIVQNKIKDFKKRKGRTTSTFKKWKWLYFWWE
|
Corresponds to the C-terminus of a putative G subtype type II restriction/methylase subunit.
|
P75453
|
T2RMN_MYCPN
|
Putative type II restriction enzyme and methyltransferase RM.MpnORF109P N-terminus
|
MKFKLNFHEKINQKDCWQSLIDHKERSYSLDFVNNTEKELPLIYGYEVKDFENHGVKIGYTTCKPSDKIQSAIEERILSQEKEFRFLDENIEKIEEVKVIFWAIAINEKDESFKDYSLHSFIKEKNLLKESQAGGEWFIVDENKDKFEYLSQIFRQFRAPSLFKK
|
Corresponds to the N-terminus of a putative G subtype type II restriction/methylase subunit.
|
P76096
|
MOKB_ECOLI
|
Regulatory protein MokB
|
MNLAIQILASYPPSGKEKGYEAQPSGGVSAHYLHYDSDIHTPDPTNALRTAVPGR
|
Overlapping regulatory peptide whose translation enables hokB expression.
|
P77453
|
HYFJ_ECOLI
|
Hydrogenase-4 component J (EC 1.-.-.-)
|
MTEECGEIVFWTLRKKFVASSDEMPEHSSQVMYYSLAIGHHVGVIDCLNVAFRCPLTEYEDWLALVEEEQARRKMLGVMTFGEIVIDASHTALLTRAFAPLADDATSVWQARSIQFIHLLDEIVQEPAIYLMARKIA
|
Possible component of hydrogenase 4.
|
P78699
|
SOM1_KLULA
|
Protein SOM1, mitochondrial
|
MAPPTKILGLDTQQRMLQRGENCSLKSLVQNECAFNGNDYVCTPFKRLFEQCMVKDGRVLNIEVTNLNTNR
|
Required for mitochondrial inner membrane peptidase function.
|
P80173
|
48KD_BACCE
|
48 kDa protein
|
XTQQEGMDISSSLXK
|
Not known, part of the enterotoxin complex.
|
P80437
|
HPAA_STRGD
|
Hydroxypicolinic acid-activating enzyme
|
MLDGVVARPQEXAARYYAAGY
|
Involved in etamycin biosynthesis.
|
P80578
|
PEDI_HYDVU
|
Pedin
|
EELRPEVLPDVSE
|
Morphogenetically active peptide. Active in foot development.
|
P80936
|
ECD1_LYMDI
|
Testis ecdysiotropin peptide 1 (TE)
|
ISDFDEYEPLNDADNNEVLDF
|
Start or boost ecdysteroid synthesis in testis of larvae and pupae.
|
P80938
|
ECDA_LYMDI
|
Testis ecdysiotropin peptide A (TE)
|
ISALFDEYEPLNDAD
|
Stimulates synthesis of ecdysteroid in the testes of larvae and pupae.
|
P80939
|
ECDB_LYMDI
|
Testis ecdysiotropin peptide B (TE)
|
SELTVEDVEPLNNADKNKVVIXI
|
Stimulates synthesis of ecdysteroid in the testes of larvae and pupae.
|
P80940
|
ECDC_LYMDI
|
Testis ecdysiotropin peptide C (TE)
|
IAIFNAYTPLPFAD
|
Stimulates synthesis of ecdysteroid in the testes of larvae and pupae.
|
P80941
|
ECDE_LYMDI
|
Testis ecdysiotropin peptide E (TE)
|
SAIDPNPDTPDSE
|
Stimulates synthesis of ecdysteroid in the testes of larvae and pupae.
|
P80959
|
LC70_LACPA
|
Bacteriocin lactocin-705
|
GMSGYIQGIPDFLKGYLHGISAANKHKKGRL
|
Antibacterial activity against several lactic acid bacteria, Listeria, Streptococci, etc.
|
P80968
|
SMBP_RAT
|
SM-11044-binding protein
|
FVVFILADPARYFQFYFPXFFQHR
|
May mediate relaxation of depolarized colon tonus. It binds iodocyanopindolol and SM-11044.
|
P81000
|
GVPC_SPICC
|
Gas vesicle protein C (GvpC)
|
ALQDDWQQSHLERRQVLAESQKQIQATIGALXXERQXXA
|
Confers stability, involved in shaping gas vesicles, hollow, gas filled proteinaceous nanostructures. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition.
|
P81096
|
PC20_BRANA
|
20 kDa pollen coat protein
|
APLTNEYLNHLCHKC
|
Major component of the pollen coat.
|
P81411
|
LPAA_PORGN
|
Lipid-A-associated protein
|
AQGDNPDKDTDGN
|
Is associated with lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
P81473
|
LEF2_NPVAG
|
Late expression factor 2
|
MASTTVWNPAAGVGSLKNSEKYLIDPDDFVGVLALSPCTVFKQGLFVEMSGLRLRALLTATKPAEPKRAVLHRSKRNVCLKACADGSINLAKALSSLRMPLCMVKIMTELSNASAPRGGMYRKRFEFTCYLGNVVSCTKCKSACLIDALLHFYKMDPKCVGEVMHLLIKAEDVYKPSNCVKMKAVNKLCPKAGTCKGKNPICNF
|
Required for late and very late gene expression. Specifically required for expression from the vp39 and polh promoters (By similarity).
|
P81671
|
CLPA_PINPS
|
ATP-dependent Clp protease ATP-binding subunit ClpA homolog
|
AESEAGDASPLVTEVLIGSPPGYVGYTEGG
|
May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.
|
P81707
|
PLP_BRANA
|
Plastidial lipid-associated protein
|
VIDVNDEW
|
May play a structural role in the elaioplast, a tapetum-specific plastidial lipid organelle.
|
P81870
|
LEAH_PHAVU
|
Putative alpha-amylase inhibitor
|
XXXGLXIVDAFVQPNLILQGDAKVEDNGXL
|
Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects (By similarity).
|
P82004
|
V25K_WSSV
|
25 kDa structural polyprotein
|
MDLSFTLSVVTA
|
Structural component of the virion.
|
P82005
|
V23K_WSSV
|
23 kDa structural polyprotein
|
MEFGNLTNLDVA
|
Structural component of the virion.
|
P82006
|
V14K_WSSV
|
14.5 kDa structural polyprotein
|
VARGGKTKGRRG
|
Structural component of the virion.
|
P82353
|
NLTP2_PRUAR
|
Non-specific lipid-transfer protein 2 (LTP 2)
|
VTCSPVQLSPCLGPINSGAPSPTTCCQKLREQRPCLCGYLKNPSLRQYVNSPNARKLASNCGVPVPQC
|
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
|
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