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 01-MAY-2013, entry version 52.
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; MNTVEFI; -.
DR ProtClustDB; CLSK791816; -.
DR BioCyc; MSP164756:GHQ8-3756-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; 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; PF00668; Condensation; 1.
DR Pfam; PF08415; NRPS; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF47336; ACP_like; 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 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
//
