MBTB_MYCSS
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 03-AUG-2022, entry version 94.
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; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified 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., Pitluck S.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Miller C.D., Hughes J.E., Anderson A.J., 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 biosynthetic
CC pathway. Putatively couples activated salicylic acid with serine or
CC threonine and cyclizes this precursor to the hydroxyphenyloxazoline
CC ring system present in this class of siderophores (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000250};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC -!- DOMAIN: Modular protein that contains an aryl carrier protein (ArCP)
CC domain which bears a phosphopantetheinyl arm to attach the activated
CC salicylic acid, a condensation/cyclization domain involved in the
CC formation of the oxazoline ring, an adenylation domain which activates
CC the serine or threonine residue into an aminoacyl-AMP ester, and a
CC peptidyl carrier protein (PCP) domain which bears a phosphopantetheinyl
CC arm to attach the activated serine or threonine. {ECO:0000250}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC in each of the two carrier protein domains, leading to their activation
CC from apo to holo forms. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC MbtB subfamily. {ECO:0000305}.
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DR EMBL; CP000384; ABG09577.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1B6A7; -.
DR SMR; Q1B6A7; -.
DR KEGG; mmc:Mmcs_3470; -.
DR HOGENOM; CLU_000022_2_4_11; -.
DR OMA; MNTVEFI; -.
DR BioCyc; MSP164756:G1G6O-3540-MON; -.
DR UniPathway; UPA00011; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..1167
FT /note="Phenyloxazoline synthase MbtB"
FT /id="PRO_0000261308"
FT DOMAIN 2..78
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1054..1130
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 78..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..390
FT /note="Condensation/cyclization"
FT REGION 575..967
FT /note="Adenylation"
FT MOD_RES 39
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1089
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
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
