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Database: UniProt
Entry: Q1B6A7
LinkDB: Q1B6A7
Original site: Q1B6A7 
ID   MBTB_MYCSS              Reviewed;        1167 AA.
AC   Q1B6A7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   19-FEB-2014, entry version 57.
DE   RecName: Full=Phenyloxazoline synthase MbtB;
DE            EC=6.3.2.-;
DE   AltName: Full=Mycobactin synthetase protein B;
GN   Name=mbtB; OrderedLocusNames=Mmcs_3470;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the initial steps of the mycobactin
CC       biosynthetic pathway. Putatively couples activated salicylic acid
CC       with serine or threonine and cyclizes this precursor to the
CC       hydroxyphenyloxazoline ring system present in this class of
CC       siderophores (By similarity).
CC   -!- COFACTOR: Binds 2 phosphopantetheines covalently (By similarity).
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- DOMAIN: Modular protein that contains an aryl carrier protein
CC       (ArCP) domain which bears a phosphopantetheinyl arm to attach the
CC       activated salicylic acid, a condensation/cyclization domain
CC       involved in the formation of the oxazoline ring, an adenylation
CC       domain which activates the serine or threonine residue into an
CC       aminoacyl-AMP ester, and a peptidyl carrier protein (PCP) domain
CC       which bears a phosphopantetheinyl arm to attach the activated
CC       serine or threonine (By similarity).
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
CC       serine in each of the two carrier protein domains, leading to
CC       their activation from apo to holo forms (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. MbtB subfamily.
CC   -!- SIMILARITY: Contains 2 acyl carrier domains.
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DR   EMBL; CP000384; ABG09577.1; -; Genomic_DNA.
DR   RefSeq; YP_640633.1; NC_008146.1.
DR   ProteinModelPortal; Q1B6A7; -.
DR   STRING; 164756.Mmcs_3470; -.
DR   EnsemblBacteria; ABG09577; ABG09577; Mmcs_3470.
DR   GeneID; 4112302; -.
DR   KEGG; mmc:Mmcs_3470; -.
DR   PATRIC; 18117237; VBIMycSp106721_3558.
DR   eggNOG; COG3433; -.
DR   HOGENOM; HOG000217264; -.
DR   KO; K04788; -.
DR   OMA; ETTIWNI; -.
DR   OrthoDB; EOG6W71XK; -.
DR   ProtClustDB; CLSK791816; -.
DR   BioCyc; MSP164756:GHQ8-3502-MONOMER; -.
DR   UniPathway; UPA00011; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013624; NRPS.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF08415; NRPS; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ligase; Multifunctional enzyme; Phosphopantetheine;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1167       Phenyloxazoline synthase MbtB.
FT                                /FTId=PRO_0000261308.
FT   DOMAIN        7     75       Acyl carrier 1.
FT   DOMAIN     1055   1127       Acyl carrier 2.
FT   REGION       98    390       Condensation/cyclization.
FT   REGION      575    967       Adenylation.
FT   MOD_RES      39     39       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    1089   1089       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
SQ   SEQUENCE   1167 AA;  125554 MW;  C9FF923084FA4A0F CRC64;
     MEAVVTSSQT VRAEVAELLG IEESALDPDA DLIASGLDSI RMMSLSGRWR KQGIDVRFAA
     MAANPTVAAW TRLVGERTAE SPGAATQSGD TAASAGDPDA PFPLAPIQHA LWVGRNELTE
     LGGVAAHLYV EFDGAGVDPE RLRTAAAALA ARHPMLRVDI LGDGMQRISD RDLPVKVTDL
     RHLDVADAEQ QLEVIRHAKS HQLLEGEVLE LALTLLPDGR TRLHVDLDMQ AADAVSYRNF
     MADLAALYRG AQLPELQYTY RQYRSAFTAT PAPTVDEDRR WWTERIPDLP EPPALPLVPR
     AEQRDPRRGT RRWHFLDTDI RDRLFAAARA RGITPAMAFA ASYAGTLARW STSRHFLLNL
     PMFGREPFHP DVDKLVGDFT SSLMLDVDFT EAHTPAQRAR VMQEALHTSA EHATYSGLSV
     LRDLSRHHGS PSLAPFVFTS ALGLGDLFAG DVTDQFGTPV WHISQGPQVL LDAQVTPFDG
     GLLVNWDVRE DAFRPGVIDA MFAYQLAELE RLAADDAAWD AADPPAVPPA QRAVRDAVND
     TGARRSDDAL HDGFFRTAAH TPDATAVIGS TGTLTYAELR ERVLAVTGAL QVAGIKPGDT
     VAVMGPKCAD QVTALLAIHA AGAVYVPIGA DQPADRADSI LQTAGVRMAL ACGDEPPTFL
     PALTIAEAVR VGSRVHGVTP ATVEPDRVAY VLFTSGSTGA PKGVEVTHAA AMNTLEFIND
     HFGIGPSDRS LALSTLEGDL SVLDVFGMLR AGGSLVVVDE AQRRDPDSWA RLIAEHSVTV
     LHWMPGWLEM LLEVGGALPS VRVVPTGGDW VRTEMVRELR RAAPGVRFAG LGGATETAIH
     NTICEPGELP REWSAVPFGR PLPNNACRVV AADGADCPDW VPGELWVGGR GIARGYRGRP
     DLTAERFVVH DGRTWYRTGD LVRYLPDGQI DFVGRADHRV KISGYRIELG EVEAALRRIA
     GVEAAVAAVL TAPGDGRGEQ LAAIVRASSP AVTVDELTRR MAELVPPHMV PSHIALVEAV
     PFTVGGKIDR RAVTAELTRS MAERANAQAP TYRVPSTALE RALADIVSTV LDRDSVGADD
     DFFELGGDSV LATQAVARIR EWLDSPGVMV TDIFAARRVG ALARRLVDHE SGSDRLEGVA
     ELYLEVADMN SADVASALHS TSAQASR
//
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