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MBTB_MYCTO
ID   MBTB_MYCTO              Reviewed;        1414 AA.
AC   P9WQ62; L0TCD0; P71717; Q7D788;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Phenyloxazoline synthase MbtB;
DE            EC=6.3.2.-;
DE   AltName: Full=Mycobactin synthetase protein B;
GN   Name=mbtB; OrderedLocusNames=MT2451;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   FUNCTION, DOMAIN, AND PHOSPHOPANTETHEINYLATION AT SER-39 AND SER-1094.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=9831524; DOI=10.1016/s1074-5521(98)90291-5;
RA   Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.;
RT   "Identification of a Mycobacterium tuberculosis gene cluster encoding the
RT   biosynthetic enzymes for assembly of the virulence-conferring siderophore
RT   mycobactin.";
RL   Chem. Biol. 5:631-645(1998).
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. Essential for growth
CC       in macrophages. {ECO:0000269|PubMed:9831524}.
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, a peptidyl
CC       carrier protein (PCP) domain which bears a phosphopantetheinyl arm to
CC       attach the activated serine or threonine, and a terminal thioesterase
CC       domain which assists in the transfer of intermediates from MbtB to ACP1
CC       in MbtD. {ECO:0000269|PubMed:9831524}.
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.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MbtB subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46746.1; -; Genomic_DNA.
DR   PIR; B70674; B70674.
DR   RefSeq; WP_010924520.1; NC_002755.2.
DR   AlphaFoldDB; P9WQ62; -.
DR   SMR; P9WQ62; -.
DR   ESTHER; myctu-MBTB; Thioesterase.
DR   EnsemblBacteria; AAK46746; AAK46746; MT2451.
DR   KEGG; mtc:MT2451; -.
DR   HOGENOM; CLU_000022_2_4_11; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001020; Chromosome.
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:0008610; P:lipid 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; -; 2.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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; 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   InterPro; IPR001031; Thioesterase.
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   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT   CHAIN           1..1414
FT                   /note="Phenyloxazoline synthase MbtB"
FT                   /id="PRO_0000426831"
FT   DOMAIN          5..78
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1057..1135
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          96..394
FT                   /note="Condensation/cyclization"
FT   REGION          579..975
FT                   /note="Adenylation"
FT   REGION          1188..1413
FT                   /note="Thioesterase"
FT   MOD_RES         39
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:9831524"
FT   MOD_RES         1094
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:9831524"
SQ   SEQUENCE   1414 AA;  151634 MW;  128EEE40E071CB1D CRC64;
     MVHATACSEI IRAEVAELLG VRADALHPGA NLVGQGLDSI RMMSLVGRWR RKGIAVDFAT
     LAATPTIEAW SQLVSAGTGV APTAVAAPGD AGLSQEGEPF PVAPMQHAMW VGRHDHQQLG
     GVAGHLYVEF DGARVDPDRL RAAATRLALR HPMLRVQFLP DGTQRIPPAA GSRDFPISVA
     DLRHVAPDVV DQRLAGIRDA KSHQQLDGAV FELALTLLPG ERTRLHVDLD MQAADAMSYR
     ILLADLAALY DGREPPALGY TYREYRQAIE AEETLPQPVR DADRDWWAQR IPQLPDPPAL
     PTRAGGERDR RRSTRRWHWL DPQTRDALFA RARARGITPA MTLAAAFANV LARWSASSRF
     LLNLPLFSRQ ALHPDVDLLV GDFTSSLLLD VDLTGARTAA ARAQAVQEAL RTAAGHSAYP
     GLSVLRDLSR HRGTQVLAPV VFTSALGLGD LFCPDVTEQF GTPGWIISQG PQVLLDAQVT
     EFDGGVLVNW DVREGVFAPG VIDAMFTHQV DELLRLAAGD DAWDAPSPSA LPAAQRAVRA
     ALNGRTAAPS TEALHDGFFR QAQQQPDAPA VFASSGDLSY AQLRDQASAV AAALRAAGLR
     VGDTVAVLGP KTGEQVAAVL GILAAGGVYL PIGVDQPRDR AERILATGSV NLALVCGPPC
     QVRVPVPTLL LADVLAAAPA EFVPGPSDPT ALAYVLFTSG STGEPKGVEV AHDAAMNTVE
     TFIRHFELGA ADRWLALATL ECDMSVLDIF AALRSGGAIV VVDEAQRRDP DAWARLIDTY
     EVTALNFMPG WLDMLLEVGG GRLSSLRAVA VGGDWVRPDL ARRLQVQAPS ARFAGLGGAT
     ETAVHATIFE VQDAANLPPD WASVPYGVPF PNNACRVVAD SGDDCPDWVA GELWVSGRGI
     ARGYRGRPEL TAERFVEHDG RTWYRTGDLA RYWHDGTLEF VGRADHRVKI SGYRVELGEI
     EAALQRLPGV HAAAATVLPG GSDVLAAAVC VDDAGVTAES IRQQLADLVP AHMIPRHVTL
     LDRIPFTDSG KIDRAEVGAL LAAEVERSGD RSAPYAAPRT VLQRALRRIV ADILGRANDA
     VGVHDDFFAL GGDSVLATQV VAGIRRWLDS PSLMVADMFA ARTIAALAQL LTGREANADR
     LELVAEVYLE IANMTSADVM AALDPIEQPA QPAFKPWVKR FTGTDKPGAV LVFPHAGGAA
     AAYRWLAKSL VANDVDTFVV QYPQRADRRS HPAADSIEAL ALELFEAGDW HLTAPLTLFG
     HCMGAIVAFE FARLAERNGV PVRALWASSG QAPSTVAASG PLPTADRDVL ADMVDLGGTD
     PVLLEDEEFV ELLVPAVKAD YRALSGYSCP PDVRIRANIH AVGGNRDHRI SREMLTSWET
     HTSGRFTLSH FDGGHFYLND HLDAVARMVS ADVR
 
 
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