VABF_VIBAN
ID VABF_VIBAN Reviewed; 2835 AA.
AC Q0E7C4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Vanchrobactin synthase VabF {ECO:0000305};
DE EC=6.2.1.63 {ECO:0000305|PubMed:17159203};
DE EC=6.2.1.72 {ECO:0000305|PubMed:17159203};
DE AltName: Full=L-arginine--[L-arginyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=L-serine--[L-seryl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Nonribosomal peptide synthase VabF {ECO:0000305};
GN Name=vabF {ECO:0000303|PubMed:17159203};
OS Vibrio anguillarum (Listonella anguillarum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=55601;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=RV22 / Serotype O2;
RX PubMed=17159203; DOI=10.1099/mic.0.29298-0;
RA Balado M., Osorio C.R., Lemos M.L.;
RT "A gene cluster involved in the biosynthesis of vanchrobactin, a
RT chromosome-encoded siderophore produced by Vibrio anguillarum.";
RL Microbiology 152:3517-3528(2006).
CC -!- FUNCTION: Involved in the synthesis of the siderophore vanchrobactin
CC (PubMed:17159203). Probably adenylates L-arginine via its first
CC adenylation domain and loads it onto its first peptidyl carrier domain
CC via a thioester linkage to the phosphopanthetheine moiety. In addition,
CC may adenylate L-serine via its second adenylation domain and loads it
CC onto its second peptidyl carrier domain via a thioester linkage to the
CC phosphopanthetheine moiety (Probable). The thioesterase domain may
CC release vanchrobactin after condensation of the siderophore components
CC (Probable). {ECO:0000269|PubMed:17159203, ECO:0000305|PubMed:17159203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-arginine = AMP +
CC diphosphate + L-arginyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:62492, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15940,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144966, ChEBI:CHEBI:456215;
CC EC=6.2.1.63; Evidence={ECO:0000305|PubMed:17159203};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62493;
CC Evidence={ECO:0000305|PubMed:17159203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-serine = AMP +
CC diphosphate + L-seryl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61704, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15913,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144955, ChEBI:CHEBI:456215;
CC EC=6.2.1.72; Evidence={ECO:0000305|PubMed:17159203};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61705;
CC Evidence={ECO:0000305|PubMed:17159203};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17159203}.
CC -!- DOMAIN: Modular protein that contains two adenylation domains which
CC activate the amino acids into aminoacyl-AMP esters, two peptidyl
CC carrier protein domains which bear a phosphopantetheinyl arm to attach
CC the activated amino acids, three condensation domains and a
CC thioesterase domain that may release the newly synthesized peptide from
CC the enzyme. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant can still produce DHBA, but not
CC vanchrobactin. Mutant is significantly impaired for growth under iron-
CC limited conditions, and siderophore levels in supernatants are less
CC than 20% of those detected in the parental strain.
CC {ECO:0000269|PubMed:17159203}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AM168450; CAJ45639.1; -; Genomic_DNA.
DR KEGG; ag:CAJ45639; -.
DR BioCyc; MetaCyc:MON-20477; -.
DR BRENDA; 6.2.1.63; 17127.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 3.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..2835
FT /note="Vanchrobactin synthase VabF"
FT /id="PRO_0000454850"
FT DOMAIN 988..1062
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2503..2578
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 16..452
FT /note="Condensation 1"
FT /evidence="ECO:0000305"
FT REGION 473..880
FT /note="Adenylation 1"
FT /evidence="ECO:0000305"
FT REGION 1081..1499
FT /note="Condensation 2"
FT /evidence="ECO:0000305"
FT REGION 1539..1961
FT /note="Condensation 3"
FT /evidence="ECO:0000305"
FT REGION 1992..2394
FT /note="Adenylation 2"
FT /evidence="ECO:0000305"
FT REGION 2601..2821
FT /note="Thioesterase"
FT /evidence="ECO:0000305"
FT MOD_RES 1023
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2538
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2835 AA; 316539 MW; 2A7FD703B3D29E24 CRC64;
MTFVRNKEMH NSSVQEDQWP LIGTQQGIWF AEQMMPNPEQ FNVAHYVVIQ GQIDIELFSN
AVAIGLQGVD SLHCHYLESD GSVRQQFYPA DEEGQWLESS TFHKPPCQKS RLGKWMKHDL
RSGWTFSKKE RFRHCLIDVG SSNAPQWFWY QRYHHIDVDG FSVNAISQYI CQLYKHWRIG
AAKPQEFSAF SDVIQEYQQF LDSAARQQAY DFWQTQAAHL PNVISLTTGS AANTSSSTIT
HTVPLIGGEW LTRYNPQLLP AELAMAMVFA YLHLHSGQEQ VCVGVPFMRR MGNAATCAAG
AVVNVLPVAL SLHPQMSIID VAREMNKTIR QVRRHQMYDA EQIQRDLGLV GQPLYGPILN
FKPFEAALSL SGVETETHIL SAGPIDEIEF SPVLDGQTLS VNITANSTKY SQESLELHAA
RFVAMVEQIA NHPTQPLDLV ELIPPSEKQQ ITLWSVGPQH EHGTEQTVLD VWQQTVESKP
NEDALVFKQQ RWTFDAFNHL IETRADQLIT AGLRQGDIAG VALRRGPESV VTMLAILRAG
AIYLPIDLDY PIERIESIVE QARPWCLVVE EDEQNMAYSS ISYVPRFIAL PELARIHTAP
QPKPTISHSD VAYIIFTSGS TGHPKGVMNT HGALLNLLRS HQGSIFSAAI RKLATRRQLP
EQAITVRAAH TTSFSFDASW EQVLWMLSGH TMYLYDDEQR KDAYELVQCV AEDNIDALDL
PPSLFDQMLD SGLITNDHVP TLVLIGSEAI PQKLWSRVSE FPELLVENFY GPTEFTVDAI
SASLDADASP VIGRPIAGAC VYVLDENLEP VAIGEVGELY LSGAGLAKGY LNQPSMTAER
FVANPFAYGK IMYRTGDLVK WRDNGLLDFV GRCDHQIKIR GFRIELGDVE SAINAIDGVN
TTVVVAEPVG DTHRLLAYCT LEKGAQGESV QPAFTEQRLQ SLIAQALPDY MQPANVMILD
AFSLNVNGKI DRKALPKYSA GMRSERVAPI TQPEQLLCDA ITELLGVSDV GMSDDFFNLG
GDSISAMSLG TRLRTAGYDL RPKAIFAARQ LGMMAGQMVP LQQQQREKQE GIIRPLPMWQ
WFEETFSITT SYVQSVLVEV ESDTQLAHLQ ASLVQLVANH SVCRLVQKEQ QYHIEALQNL
DVKNWVESVS VERLDGQRWW TVCLAQRSQS MSISSGQLLR LVMITERSGR KISDLAHHFL
IDGVSWRICF RSCRHLTQAQ VTGEVAVISE EVTGIHCWSK ALYQHLAVAA AQMPFWRAQA
QRAVAPIKDP VDKIRMTHWR TPLSHAVTQP LLELPTHQTN LDIEEMLLAA VTGVIARLYG
CEEIKVNVES HGREECKEEI DLNQTLGWFT TEYPLIINVP KQGDYRERLR EVKQSKRSVK
DKGLGYMVLR YLDNPYRDEL RTLANTRQPS LLFNYLGRFQ SSDGQWSPQQ YSGQFADTFA
VTLNSERALQ HPLELNIFVE ESATPRLVLN WSWNAHLFSQ QEMVSLSQQI ESELLKIQQA
LQVGDSAELD LSVPADYTEP GITLRQASLL QHHYGKLADV LPALPLQEGL LFQSQLGDKN
SSYNSTTRLT FQGQLSEHRV SEALNAVIRR HPQLLARFDS SILGRTVQVM TQVNPSWPLT
RYDITNMSGD EQSALIDQLE KQELSRQFDL NDSTHSLLQA QLIFHGDQQS TLLLSAHHLV
VDGWSTPILL NDFLSAYAQG VSNLPPVTVG YAHVVSQLTQ RDKTVATELW GKVLADVQPS
MAFDDIPLSE EVNEHQLWLS KHKTDQLNQC LRHHGLTMST LMQGLWASIL ASMTGREEVV
FGTPISGRFS RIAGIDEQIG LFSNTVPVRV TLQPHLSLSE QLEAHQAIQI QLLEHDELGL
GEIQQLVGGK TLFDTLLVVE NYPDHSRWYQ QDFSGAKLMA IHNRGYTHYP LTILVLPGEQ
LHILFEYRDR VGVAKQIVQR FEQMLDEFMV SSDKPFAEWD LRLSGEIELQ QRVNQTKTAV
ERTTLRDLMI TQQQRSPHQL ALIDSEHRFT YQALAEQVAA IADLLLQQGI KAGDIVAVAL
PRSATLSLAI YSIIECGAAY LPLDVGYPDE RLAYMINDAK PALIITCSSF TSRFEALAAL
LLLDKLPAPV RAERQNRADG LTPSNAAYLL YTSGSTGNPK GVLVSHQAIV NRLKWMQHQY
PLNSEDVVLQ KTPCSFDVSV WEFFWPLLEG ASLVMAPAEA HKDPEWLLQI IDDYHVTTMH
FVPSMLAAFM ASIEATHPTG FTVAPSLKQV FCSGEALAKE LCHQYARRIN APLHNLYGPT
EAAVDVTYYP AYGEALNASV GRSAPIGLPV WNTQVYVLDS FLRAVPIGVP GELYLAGEQL
AIGYFNRSAL TADRFIANPF TCGERMYRTG DVVRWLACGS IEYLGRSDDQ IKIRGQRVEL
GEIGSALQAL PAVKQAVVCA QTLSTHSGML GADERQIIGY VIAHDMSVTN GEKLRTELSE
HLPAHMVPAA IVLLDHYPLS ANGKLDKKAL PRPNDVAVRV GRNAHPGLET QLVTLFAQVL
AVETLFADDD FLTLGGHSLL AMKLAADIRR ALNLPVTVGQ IMVNPTVEKL ASLLLDDDAF
NDPTLAGFGE VLPIRAGSGP ALFCVNSASG FAWQYTGLPK YLTGHYPIYG LQSPRPGGAM
ATSETMEEVC DRLLPVLREI QPFGPYHLLG YSFGGIVAQK LAAKLQQQGE EVHFLGLLDT
YPPEGQNWDG PMDEEKQYEI EREKEQFLAI NELTDIELDE QRLAMFNEIT ANYEDAVRLL
AQAQTSDYQG PAHLFVAQRT VPDGYDIDAH WQSFVGQLIK HQFDCSHEDI LAPENVRQIG
ECLNTLLESK AALKK
