entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
P0A5F0
|
MAZE1_MYCBO
|
Probable antitoxin MazE1
|
MPFLVALSGIISGVRDHSMTVRLDQQTRQRLQDIVKGGYRSANAAIVDAINKRWEALHDEQLDAAYAAAIHDNPAYPYESEAERSAARARRNARQQRSAQ
|
Probable antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to cognate MazF1 toxin and counteracts its endoribonuclease activity.
|
P0A8C9
|
YIDD_SALTY
|
Putative membrane protein insertion efficiency factor
|
MAPPLSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
P0A8U1
|
SYDP_ECOL6
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function (By similarity).
|
P0A8Z8
|
YQIA_ECOL6
|
Esterase YqiA (EC 3.1.-.-)
|
MSTLLYLHGFNSSPRSAKASLLKNWLAEHHPDVEMIIPQLPPYPSDAAELLESIVLEHGGDSLGIVGSSLGGYYATWLSQCFMLPAVVVNPAVRPFELLTDYLGQNENPYTGQQYVLESRHIYDLKVMQIDPLEAPDLIWLLQQTGDEVLDYRQAVAYYASCRQTVIEGGNHAFTGFEDYFNPIVDFLGLHHL
|
Displays esterase activity toward palmitoyl-CoA and pNP-butyrate.
|
P0A8Z9
|
YQIA_ECO57
|
Esterase YqiA (EC 3.1.-.-)
|
MSTLLYLHGFNSSPRSAKASLLKNWLAEHHPDVEMIIPQLPPYPSDAAELLESIVLEHGGDSLGIVGSSLGGYYATWLSQCFMLPAVVVNPAVRPFELLTDYLGQNENPYTGQQYVLESRHIYDLKVMQIDPLEAPDLIWLLQQTGDEVLDYRQAVAYYASCRQTVIEGGNHAFTGFEDYFNPIVDFLGLHHL
|
Displays esterase activity toward palmitoyl-CoA and pNP-butyrate.
|
P0A900
|
YQIA_SHIFL
|
Esterase YqiA (EC 3.1.-.-)
|
MSTLLYLHGFNSSPRSAKASLLKNWLAEHHPDVEMIIPQLPPYPSDAAELLESIVLEHGGDSLGIVGSSLGGYYATWLSQCFMLPAVVVNPAVRPFELLTDYLGQNENPYTGQQYVLESRHIYDLKVMQIDPLEAPDLIWLLQQTGDEVLDYRQAVAYYASCRQTVIEGGNHAFTGFEDYFNPIVDFLGLHHL
|
Displays esterase activity toward palmitoyl-CoA and pNP-butyrate.
|
P0AAB9
|
USPD_SHIFL
|
Universal stress protein D
|
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKMSADLLIVPFIDK
|
Required for resistance to DNA-damaging agents.
|
P0AAY2
|
BSSR_ECO57
|
Biofilm regulator BssR
|
MFVDRQRIDLLNRLIDARVDLAAYVQLRKAKGYMSVSESNHLRDNFFKLNRELHDKSLRLNLHLDQEEWSALHHAEEALATAAVCLMSGHHDCPTVITVNADKLENCLMSLTLSIQSLQKHAMLEKA
|
Represses biofilm formation in M9C glu and LB glu media but not in M9C and LB media. Seems to act as a global regulator of several genes involved in catabolite repression and stress response and regulation of the uptake and export of signaling pathways. Could be involved the regulation of indole as well as uptake and export of AI-2 through a cAMP-dependent pathway (By similarity).
|
P0AAY3
|
BSSR_SHIFL
|
Biofilm regulator BssR
|
MFVDRQRIDLLNRLIDARVDLAAYVQLRKAKGYMSVSESNHLRDNFFKLNRELHDKSLRLNLHLDQEEWSALHHAEEALATAAVCLMSGHHDCPTVITVNADKLENCLMSLTLSIQSLQKHAMLEKA
|
Represses biofilm formation in M9C glu and LB glu media but not in M9C and LB media. Seems to act as a global regulator of several genes involved in catabolite repression and stress response and regulation of the uptake and export of signaling pathways. Could be involved the regulation of indole as well as uptake and export of AI-2 through a cAMP-dependent pathway (By similarity).
|
P0AB29
|
YCED_ECOL6
|
Large ribosomal RNA subunit accumulation protein YceD (23S rRNA accumulation protein YceD)
|
MQKVKLPLTLDPVRTAQKRLDYQGIYTPDQVERVAESVVSVDSDVECSMSFAIDNQRLAVLNGDAKVTVTLECQRCGKPFTHQVYTTYCFSPVRSDEQAEALPEAYEPIEVNEFGEIDLLAMVEDEIILALPVVPVHDSEHCEVSEADMVFGELPEEAQKPNPFAVLASLKRK
|
Plays a role in synthesis, processing and/or stability of 23S rRNA.
|
P0AB30
|
YCED_ECO57
|
Large ribosomal RNA subunit accumulation protein YceD (23S rRNA accumulation protein YceD)
|
MQKVKLPLTLDPVRTAQKRLDYQGIYTPDQVERVAESVVSVDSDVECSMSFAIDNQRLAVLNGDAKVTVTLECQRCGKPFTHQVYTTYCFSPVRSDEQAEALPEAYEPIEVNEFGEIDLLAMVEDEIILALPVVPVHDSEHCEVSEADMVFGELPEEAQKPNPFAVLASLKRK
|
Plays a role in synthesis, processing and/or stability of 23S rRNA.
|
P0AB34
|
BSSS_ECOL6
|
Biofilm regulator BssS
|
MEKNNEVIQTHPLVGWDISTVDSYDALMLRLHYQTPNKSEQEGTEVGQTLWLTTDVARQFISILEAGIAKIESGDFQVNEYRRH
|
Represses biofilm formation in M9C glu and LB glu media but not in M9C and LB media. Seems to act as a global regulator of several genes involved in catabolite repression and stress response and regulation of the uptake and export of signaling pathways. Could be involved the regulation of indole as well as uptake and export of AI-2 through a cAMP-dependent pathway (By similarity).
|
P0ABR3
|
DINI_ECO57
|
DNA damage-inducible protein I
|
MRIEVTIAKTSPLPAGAIDALAGELSRRIQYAFPDNEGHVSVRYAAANNLSVIGATKEDKQRISEILQETWESADDWFVSE
|
Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA (By similarity).
|
P0ABR4
|
DINI_SHIFL
|
DNA damage-inducible protein I
|
MRIEVTIAKTSPLPAGAIDALAGELSRRIQYAFPDNEGHVSVRYAAANNLSVIGATKEDKQRISEILQETWESADDWFVSE
|
Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA (By similarity).
|
P0AC74
|
EBGC_ECOL6
|
Evolved beta-galactosidase subunit beta
|
MRIIDNLEQFRQIYASGKKWQRCVEAIENIDNIQPGVAHSIGDSLTYRVETDSATDALFTGHRRYFEVHYYLQGQQKIEYAPKETLQVVEYYRDETDREYLKGCGETVEVHEGQIVICDIHEAYRFICNNAVKKVVLKVTIEDGYFHNK
|
Required for full activity of the EbgA enzyme. Exact function not known (By similarity).
|
P0AD73
|
LPF_SHIFL
|
phe operon leader peptide (phe operon attenuator peptide)
|
MKHIPFFFAFFFTFP
|
This protein is involved in control of the biosynthesis of phenylalanine.
|
P0AD80
|
LPL_ECOL6
|
leu operon leader peptide (leu operon attenuator peptide)
|
MTHIVRFIGLLLLNASSLRGRRVSGIQH
|
Involved in control of the biosynthesis of leucine.
|
P0AD81
|
LPL_ECO57
|
leu operon leader peptide (leu operon attenuator peptide)
|
MTHIVRFIGLLLLNASSLRGRRVSGIQH
|
Involved in control of the biosynthesis of leucine.
|
P0AD82
|
LPL_SHIFL
|
leu operon leader peptide (leu operon attenuator peptide)
|
MTHIVRFIGLLLLNASSLRGRRVSGIQH
|
Involved in control of the biosynthesis of leucine.
|
P0AD93
|
LPW_ECOL6
|
trp operon leader peptide
|
MKAIFVLKGWWRTS
|
This protein is involved in control of the biosynthesis of tryptophan.
|
P0AD94
|
LPW_ECO57
|
trp operon leader peptide
|
MKAIFVLKGWWRTS
|
This protein is involved in control of the biosynthesis of tryptophan.
|
P0AD95
|
LPW_SHIFL
|
trp operon leader peptide
|
MKAIFVLKGWWRTS
|
This protein is involved in control of the biosynthesis of tryptophan.
|
P0ADH1
|
INSA_SALTI
|
Insertion element IS1 protein InsA
|
MASVSISCPSCSATDGVVRNGKSTAGHQRYLCSHCRKTWQLQFTYTASQPGTHQKIIDMAMNGVGCRATARIMGVGLNTILRHLKNSGRSR
|
Absolutely required for transposition of IS1.
|
P0AE29
|
AROM_SHIFL
|
Protein AroM
|
MSASLAILTIGIVPMQEVLPLLTEYIDEDNISHHSLLGKLSREEVMAEYAPEAGEDTILTLLNDNQLAHVSRRKVERDLQGVVEVLDNQGYDVILLMSTANISSMTARNTIFLEPSRILPPLVSSIVEDHQVGVIVPVEEMLPVQAQKWQILQKSPVFSLGNPIHDSEQKIIDAGKELLAKGADVIMLDCLGFHQRHRDLLQKQLDVPVLLSNVLIARLAAELLV
|
This protein of unknown function is encoded by a gene that cotranscribes with the aroL gene, which codes for shikimate kinase II.
|
P0AE59
|
CAIF_SHIFL
|
Transcriptional activatory protein CaiF
|
MCEGYVEKPLYLLIAEWMMAENRWVIAREISIHFDIEHSKAVNTLTYILSEVTEISCEVKMIPNKLEGRGCQCQRLVKVVDIDEQIYARLRNNSREKLVGVRKTPRIPAVPLTELNREQKWQMMLSKSMRR
|
Potential transcriptional activator of carnitine metabolism.
|
P0AE64
|
CHAB_ECOL6
|
Putative cation transport regulator ChaB
|
MPYKTKSDLPESVKHVLPSHAQDIYKEAFNSAWDQYKDKEDRRDDASREETAHKVAWAAVKHEYAKGDDDKWHKKS
|
Might be a regulator of the sodium-potassium/proton antiporter ChaA.
|
P0AE66
|
CHAB_SHIFL
|
Putative cation transport regulator ChaB
|
MPYKTKSDLPESVKHVLPSHAQDIYKEAFNSAWDQYKDKEDRRDDASREETAHKVAWAAVKHEYAKGDDDKWHKKS
|
Might be a regulator of the sodium-potassium/proton antiporter ChaA.
|
P0AE96
|
CSGE_ECOL6
|
Curli production assembly/transport component CsgE
|
MKRYLRWIVAAEFLFAAGNLHAVEVEVPGLLTDHTVSSIGHDFYRAFSDKWESDYTGNLTINERPSARWGSWITITVNQDVIFQTFLFPLKRDFEKTVVFALIQTEEALNRRQINQALLSTGDLAHDEF
|
May be involved in the biogenesis of curli organelles.
|
P0AE97
|
CSGE_ECO57
|
Curli production assembly/transport component CsgE
|
MKRYLRWIVAAEFLFAAGNLHAVEVEVPGLLTDHTVSSIGHDFYRAFSDKWESDYTGNLTINERPSARWGSWITITVNQDVIFQTFLFPLKRDFEKTVVFALIQTEEALNRRQINQALLSTGDLAHDEF
|
May be involved in the biogenesis of curli organelles.
|
P0AE99
|
CSGF_ECOL6
|
Curli production assembly/transport component CsgF
|
MRVKHAVVLLMLISPLSWAGTMTFQFRNPNFGGNPNNGAFLLNSAQAQNSYKDPSYNDDFGIETPSALDNFTQAIQSQILGGLLSNINTGKPGRMVTNDYIVDIANRDGQLQLNVTDRKTGQTSTIQVSGLQNNSTDF
|
May be involved in the biogenesis of curli organelles.
|
P0AEA0
|
CSGF_ECO57
|
Curli production assembly/transport component CsgF
|
MRVKHAVVLLMLISPLSWAGTMTFQFRNPNFGGNPNNGAFLLNSAQAQNSYKDPSYNDDFGIETPSALDNFTQAIQSQILGGLLSNINTGKPGRMVTNDYIVDIANRDGQLQLNVTDRKTGQTSTIQVSGLQNNSTDF
|
May be involved in the biogenesis of curli organelles.
|
P0AEA1
|
CSGF_SHIFL
|
Curli production assembly/transport component CsgF
|
MRVKHAVVLLMLISPLSWAGTMTFQFRNPNFGGNPNNGAFLLNSAQAQNSYKDPSYNDDFGIETPSALDNFTQAIQSQILGGLLSNINTGKPGRMVTNDYIVDIANRDGQLQLNVTDRKTGQTSTIQVSGLQNNSTDF
|
May be involved in the biogenesis of curli organelles.
|
P0AEV5
|
HYCA_ECO57
|
Formate hydrogenlyase regulatory protein HycA
|
MTIWEISEKADYIAQRHRRLQDQWHIYCNSLVQGITLSKARLHHAMSCAPDKELCFVLFEHFRIYVTLADGFNSHTIEYYVETKDGEDKQRIAQAQLSIDGMIDGKVNIRDREQVLEHYLEKIAGVYDSLYTAIENNVPVNLSQLVKGQSPAA
|
Regulatory protein for the formate hydrogenlyase system. Could act by directly interacting with FhlA or by preventing the binding of FhlA to the upstream activatory sequence (By similarity).
|
P0AEV6
|
HYCA_SHIFL
|
Formate hydrogenlyase regulatory protein HycA
|
MTIWEISEKADYIAQRHRRLQDQWHIYCNSLVQGITLSKARLHHAMSCAPDKELCFVLFEHFRIYVTLADGFNSHTIEYYVETKDGEDKQRIAQAQLSIDGMIDGKVNIRDREQVLEHYLEKIAGVYDSLYTAIENNVPVNLSQLVKGQSPAA
|
Regulatory protein for the formate hydrogenlyase system. Could act by directly interacting with FhlA or by preventing the binding of FhlA to the upstream activatory sequence (By similarity).
|
P0AEV8
|
HYCH_ECO57
|
Formate hydrogenlyase maturation protein HycH
|
MSEKVVFSQLSRKFIDENDATPAEAQQVVYYSLAIGHHLGVIDCLEAALTCPWDEYLAWIATLEAGSEARRKMEGVPKYGEIVIDINHVPMLANAFDKARAAQTSQQQEWSTMLLSMLHDIHQENAIYLMVRRLRD
|
Seems to be required for the conversion of a precursor form of the large subunit of hydrogenlyase (HycE) into a mature form.
|
P0AFA6
|
NFRB_ECO57
|
Bacteriophage N4 adsorption protein B
|
MDWLLDVFATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGNMAELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFILHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTCFSRRAVTALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSTAVRQKSRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMIQLLLLLAYESLWPDAWHFLSIFSGSAWLMTLLWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQHGDPRRVAWDKTTHDFPSVTGDTRSLRPLGQILLENQVITEEQLDTALRNRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPASVALHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRRGHDPRAMLYNAVQHQWLTEQQAGEIWRQYVPHQFLFAEILTTLGHINRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRVLTIQRELQVSMQSLLLKAGLNTEQVAQLESENEGE
|
Required for bacteriophage N4 adsorption. May be a component of the phage receptor (By similarity).
|
P0AFW9
|
ROF_SHIFL
|
Protein rof
|
MNDTYQPINCDDYDNLELACQHHLMLTLELKDGEKLQAKASDLVSRKNVEYLVVEAAGETRELRLDKITSFSHPEIGTVVVSES
|
Suppresses temperature-sensitive mutations in essential genes by modulating rho-dependent transcription termination.
|
P0AFZ2
|
SSEB_SHIFL
|
Protein SseB
|
MSETKNELEDLLEKAATEPAHRPAFFRTLLESTVWVPGTAAQGEAVVEDSALDLQHWEKEDGTSVIPFFTSLEALQQAVEDEQAFVVMPVRTLFEMTLGETLFLNAKLPTGKEFMPREISLLIGEEGNPLSSQEILEGGESLILSEVAEPPAQMIDSLTTLFKTIKPVKRAFICSIKENEEAQPNLLIGIEADGDIEEIIQATGSVATDTLPGDEPIDICQVKKGEKGISHFITEHIAPFYERRWGGFLRDFKQNRII
|
May be involved in the enhancement of serine-sensitivity.
|
P0C1S2
|
NRDI_STAAU
|
Protein NrdI
|
MKIIYFSFTGNVRRFIKRTELENTLEITAENCMEPVHEPFIIVTGTIGFGEVPEPVQSFLEVNHQYIRGVAASGNRNWGLNFAKAGRTISEEYNVPLLMKFELHGKNKDVIEFKNKVGNFNENHGREKVQSY
|
Probably involved in ribonucleotide reductase function.
|
P0C2N3
|
PARD_YEREN
|
Antitoxin ParD
|
MARVTSVTLGEHLTGFVGEMIQSGRYGNISEVLRDALRLMEAREQRVQHVRDMVLAGTNAPVSHRLMDEIFSAAVKDTSV
|
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of toxin ParE (By similarity).
|
P0C2V7
|
LCRR_YEREN
|
Low calcium response locus protein R
|
MMEDPLIPWLTEHGLVCHPHTLSGTPISLGSAFQLAGLKLAWRVEIEQRRVWIVLIQRVEQRRGLKNPFAALYMLANAARAVLGPDYYLYGNVDVLAGSSLSTQRLAHFYRRWTGAKELSTGWFSLKVSQVITLSNMKKRQNNGFA
|
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 (By similarity).
|
P0C6P4
|
OMP7_STAAU
|
65 kDa membrane protein (map-ND2C)
|
AAKPLDKSSSSLHHGYSKVHVP
|
Binds various plasma and ECM-proteins.
|
P0C722
|
BRRF1_EBVG
|
Transcriptional activator BRRF1
|
MASSNRGNARPLKSFLHELYLKHYPEVGDVVHLLNTIGVDCDLPPSHPLLTAQRGLFLARVLQAVQQHKLLEDTIVPKILKKLAYFLELLSYYSPKDEQRDIAEVLDHLKTNRDLGLDDRLWALIRKLRQDRHHASVNVLMPGSDYTAVSLQYYDGISIGMRKVIADVCRSGYASMPSMTATHNLSHQLLMASGPSEEPCAWRGFFNQVLLWTVALCKFRRCIYYNYIQGSIATISQLLHLEIKALCSWIISQDGMRLFQHSRPLLTLWESVAANQEVTDAITLPDCAEYIDLLKHTKHVLENCSAMQYK
|
Enhances the ability of BRLF1 to induce lytic infection by cooperating with it to transcriptionally activate the BZLF1 promoter.
|
P0C723
|
BRRF1_EBVA8
|
Transcriptional activator BRRF1
|
MASSNRGNARPLKSFLHELYLKHYPEVGDVVHLLNTIGVDCDLPPSHPLLTAQRGLFLARVLQAVQQHKLLEDTIVPKILKKLAYFLELLSYYSPKDEQRDIAEVLDHLKTNRDLGLDDRLWALIRKLRQDRHHASVNVLMPGSDYTAVSLQYYDGISIGMRKVIADVCRSGYASMPSMTATHNLSHQLLMASGPSEEPCAWRGFFNQVLLWTVALCKFRRCIYYNYIQGSIATISQLLHLEIKALCSWIISQDGMRLFQHSRPLLTLWESVAANQEVTDAITLPDCAEYIDLLKHTKHVLENCSAMQYK
|
Enhances the ability of BRLF1 to induce lytic infection by cooperating with it to transcriptionally activate the BZLF1 promoter.
|
P0C740
|
5053R_ASFK5
|
Protein MGF 505-3R
|
MSSSLQELCRKNLPDDILPEFFDDYVLQLLGLHWQDHGSLQRTGKNQVLVQQEPIHINEALKVAASEGNFEIVELLLSWKADPRYAVVGALESKYYDLVYKYYNLIEDRHDMLPLIQNSETFERCHELNNCSLKCLFKHAVIYDKLPILQKYADYLDGWPYCNQMLFELACKKQKYNMVVWIEGVLGVGNFTILFTIAIIKRDLQLYSLGYSIILERMYSCGYDPTFLLNHYLRVVSTKGLLPFVLKTIEYGGSKEIAITLAKKYQHETILRYFETRKSQEC
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
P0C759
|
DP96R_ASFP4
|
TBK1 inhibitor DP96R
|
MSTHNNSPKEKPVDMNNISEKLDVVNNAPEKPAGANHIPEKLAEMTSSEWIAEYWKGINRGNDVPCCCPRKMTSADKKFSVFGKGYLMRSMQKDD
|
Inhibits cGAS-STING-mediated type I IFN expression and NF-kB activation by inhibiting TBK1 and IKBKB/IKKB (By similarity). Inhibits host TBK1 phosphorylation (By similarity).
|
P0C768
|
RAP1_PLRV1
|
Replication-associated protein (Rap1)
|
MTPMRITVWRERLQQMRPQRKLLKQTQQRRLLHQLQQRKLL
|
Involved in viral RNA replication.
|
P0C785
|
RAP1_PLRVW
|
Replication-associated protein (Rap1)
|
MTPMRITVWRKRLQQMRPQRKLLKQTQQRRLLHQLQQRKLLQQTSL
|
Seems to play a role in virus replication.
|
P0C7X8
|
PSMA1_STAA1
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7X9
|
PSMA1_STAA2
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y1
|
PSMA1_STAA8
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y2
|
PSMA1_STAA9
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y3
|
PSMA1_STAAB
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y4
|
PSMA1_STAAC
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y5
|
PSMA1_STAAE
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y6
|
PSMA1_STAAM
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y7
|
PSMA1_STAAN
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y8
|
PSMA1_STAAR
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Y9
|
PSMA1_STAAS
|
Phenol-soluble modulin alpha 1 peptide
|
MGIIAGIIKVIKSLIEQFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z0
|
PSMA2_STAA1
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z1
|
PSMA2_STAA2
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z3
|
PSMA2_STAA8
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z4
|
PSMA2_STAA9
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z5
|
PSMA2_STAAB
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z6
|
PSMA2_STAAC
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z7
|
PSMA2_STAAE
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z8
|
PSMA2_STAAM
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C7Z9
|
PSMA2_STAAN
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C800
|
PSMA2_STAAR
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C801
|
PSMA2_STAAS
|
Phenol-soluble modulin alpha 2 peptide
|
MGIIAGIIKFIKGLIEKFTGK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C802
|
PSMA3_STAA1
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C803
|
PSMA3_STAA2
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C805
|
PSMA3_STAA8
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C806
|
PSMA3_STAA9
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C807
|
PSMA3_STAAB
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse neutrophils, thus eliminating the main cellular defense against infection.
|
P0C808
|
PSMA3_STAAC
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C809
|
PSMA3_STAAE
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C810
|
PSMA3_STAAM
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C811
|
PSMA3_STAAN
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C812
|
PSMA3_STAAR
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNY
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C813
|
PSMA3_STAAS
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C814
|
PSMA3_STAAT
|
Phenol-soluble modulin alpha 3 peptide
|
MEFVAKLFKFFKDLLGKFLGNN
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C815
|
PSMA4_STAA1
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C816
|
PSMA4_STAA2
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C818
|
PSMA4_STAA8
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C819
|
PSMA4_STAA9
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C820
|
PSMA4_STAAB
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse neutrophils, thus eliminating the main cellular defense against infection.
|
P0C821
|
PSMA4_STAAC
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C822
|
PSMA4_STAAE
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C823
|
PSMA4_STAAM
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C824
|
PSMA4_STAAN
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C825
|
PSMA4_STAAR
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C826
|
PSMA4_STAAS
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C827
|
PSMA4_STAAT
|
Phenol-soluble modulin alpha 4 peptide
|
MAIVGTIIKIIKAIIDIFAK
|
Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection.
|
P0C8Z5
|
PSMG4_DICDI
|
Proteasome assembly chaperone 4
|
MESLRITDDLENIDPNIRIEKHIDNFEDTRIYFMFYIFKSQDSPIFIWVSDSPTFSTLSVSMKIPIEKSPVTSHLLESNSITSNDSSNSLSQRIVIKFKVQTFLSYSISQDIPEMSHFIEKTIFDLLSKYLKK
|
Chaperone protein which promotes assembly of the 20S proteasome.
|
P0C9E9
|
1001R_ASFWA
|
Protein MGF 100-1R
|
MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
P0C9F0
|
1001R_ASFK5
|
Protein MGF 100-1R
|
MVRLFYNPIKYLFYRRSCKKRLRKALKKLNFYHPPKECCQIYRLLENAPGGTYFITENMTNELIMIAKDPVDKKIKSVKLYLTGNYIKINQHYYINIYMYLMRYNQIYKYPLICFSKYSKIL
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
P0C9F1
|
1001R_ASFM2
|
Protein MGF 100-1R
|
MVRLFHNPIKCLFYRGSRKTREKKLRKSLKKLNFYHPPGDCCQIYRLLENVPGGTYFITENMTNELIMIVKDSVDKKIKSVKLNFYGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYSYCNS
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
P0C9F2
|
1001R_ASFP4
|
Protein MGF 100-1R
|
MVRLFRNPIKCIFYRRSRKIQEKKLRKSLKKLNFYHPPEDCCQIYRLLENVPGGTYFITENMTNDLIMVVKDSVDKKIKSIKLYLHGSYIKIHQHYYINIYMYLMRYTQIYKYPLICFNKYYNI
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
P0C9F3
|
1002L_ASFWA
|
Protein MGF 100-2L
|
MGNKESRYLEMCSEEAWLNIPNIFKCIFIRKLFYNKWLKYQEKKLKKSLKLLSFYHPKKDFVGIRDMLQMAPGGSYFITDNMTEEFLMLVVKHPEDGSAEFTKLCLKGSCIVIDGYYYDNLHIFISETPDIYKYPLIRYDR
|
Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
|
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