TAGA_VIBC3
ID TAGA_VIBC3 Reviewed; 1002 AA.
AC A5F398; C3LYI7; O68335; P24019; Q56595; Q9KTR9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ToxR-activated gene A lipoprotein;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=tagA; OrderedLocusNames=VC0395_A0345, VC395_0837;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-576.
RX PubMed=7883190; DOI=10.1016/0378-1119(94)00811-6;
RA Harkey C.W., Everiss K.D., Peterson K.M.;
RT "Isolation and characterization of a Vibrio cholerae gene (tagA) that
RT encodes a ToxR-regulated lipoprotein.";
RL Gene 153:81-84(1995).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68630.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABQ22076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACP08853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ22076.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP08853.1; ALT_INIT; Genomic_DNA.
DR EMBL; U12265; AAA68630.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; A5F398; -.
DR SMR; A5F398; -.
DR STRING; 345073.VC395_0837; -.
DR EnsemblBacteria; ABQ22076; ABQ22076; VC0395_A0345.
DR KEGG; vco:VC0395_A0345; -.
DR KEGG; vcr:VC395_0837; -.
DR PATRIC; fig|345073.21.peg.808; -.
DR eggNOG; ENOG502Z7RH; Bacteria.
DR HOGENOM; CLU_008787_0_0_6; -.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019503; Peptidase_M66_dom.
DR InterPro; IPR022218; TagA_dom.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF12561; TagA; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51694; PEPTIDASE_M66; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Palmitate; Protease; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..1002
FT /note="ToxR-activated gene A lipoprotein"
FT /id="PRO_0000324809"
FT DOMAIN 45..139
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 282..536
FT /note="Peptidase M66"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 1002 AA; 114646 MW; 6A239DFB6408407F CRC64;
MVVRYSLLMK VSFAILIFLV GCNENATSSN DQYLTDPDIS EQTKKPSRPI IDEKNKGVTD
TSVTIEWDKI ECEKNFSHYN VIVYRKDRIE DVITIRTRNN SVFIDDLKPN SQYSIDVSSC
LHSACSESAK IEFITLNEID YYHTTEIEKN VYGSLEGEVR FVQTHVISPE GRKNEPEIIT
GRDALILFKP SIKNSSSILM KIYSEDGLTS KVVMKSPSML PKTDQPIDID ENNKVVSYSN
SYWSAEIPWN KMKSGMSLHF EDENGNLGII ESERIKFSAP SELIIQNIDL GMLYKPRGRN
IVIKELERTA VDYFQKVPVS KLIFSDYTPI HFEKITLPNG SVYTEKSADI GGWHQGDMRE
AVGKALVSTG INNANLGIVA SSGYSQQYNR LTNHITAHTN IGYYNNGVVV HGGSGGGGIV
TLENTLHNEW SHELGHNYGL GHYVAGGTSH GPDTSWGWDG YYKRFIANFD WKRSPQSNIR
PDNQEVVKPF MDKYTYLWDA MSGGYDHQNG IISRYTLHHP YVARIIQDWL KNGAVVINND
YMVWDELKNI YVYKGTNFKV PIKKGVPVVT ILGVYDPDKI NPSQLYPPTY SNYGNIFDLE
KPRSESSLKG WQYVKDVNYL DRVNTHWHTM LVNRKEEKIC RFSYLSPKGK KFEFLGYEDI
ENKICTGSRS IHYLEDGKKN PIESKYNDYF LLSIDGDGEI SYVPDSTIGE SKICSLKMSG
TVYGAGFIKG NSCRQIDGVF MNGFQWAFTL NQSGVNSTYT WSNECVLKIK DKDNNIESIS
IPNYRIEKNQ SNKIHLNISR EKPIIDINVY CGEHELTSIK VSDNPDIKLL KGPIIVGQEH
GYTSYEPKLP SGWFKHYDNF EPKNEINHEL GKMRVNDNDE YICRFNFSDS DREMKFVGYV
SQLSESKYIC TGGSEIYYKK NDINIELSSK ENDFEWLSVR DKNLIGSKIE FDNNKTLCVL
DNRSFYGAGY LDENNRCTQD RQIHWSNGKQ WLFSTYKTMT YH
