ID   MBTB_MYCPA              Reviewed;        1165 AA.
AC   Q73XY1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phenyloxazoline synthase MbtB;
DE            EC=6.3.2.-;
DE   AltName: Full=Mycobactin synthetase protein B;
GN   Name=mbtB; OrderedLocusNames=MAP_2177c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS04494.1; -; Genomic_DNA.
DR   RefSeq; WP_010949506.1; NC_002944.2.
DR   AlphaFoldDB; Q73XY1; -.
DR   SMR; Q73XY1; -.
DR   STRING; 262316.MAP_2177c; -.
DR   EnsemblBacteria; AAS04494; AAS04494; MAP_2177c.
DR   KEGG; mpa:MAP_2177c; -.
DR   PATRIC; fig|262316.17.peg.2315; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_2_4_11; -.
DR   OMA; MNTVEFI; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000000580; 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; -; 1.
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; 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; 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;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1165
FT                   /note="Phenyloxazoline synthase MbtB"
FT                   /id="PRO_0000261307"
FT   DOMAIN          5..78
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1055..1131
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          77..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..393
FT                   /note="Condensation/cyclization"
FT   REGION          578..973
FT                   /note="Adenylation"
FT   MOD_RES         39
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1090
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1165 AA;  125043 MW;  C69D9724B1E3A2B9 CRC64;
     MVHAPARSED IREEVAELLG VDVDAVQPGS NLIGQGLDSI RIMTLAGRWR RRGIAVDFAT
     LAETPTIEAW AQLVTAGRQD TDSAAPPADS SGDPSGETEP FALAPMQHAM WVGRQDNQQL
     GGVAGHLYVE FDAGLLDSGR LRAAATALAR RHPMLRVRFL PDGTQCITPA VECGDFPVHV
     EDLRELGTDE VERRLTALRE AKSHQQLDGA VFELTVTLLP GGRSRLHVDL DMQAADAMSY
     RTLMADLAAL YRGCDLPELS YTYRQYRHAV EAQDAQPQPR RDADRDWWAR RLPELPDPPA
     LPITAGRGAN RSTRRWHWLD PQTRDALFAR AQARGITPAM ALAAGFANTL ARWSSNSRFL
     LNVPLFGRQP LHPDVDALVG DFTSSLLLDV DLVGAHTAAA RAQVVQDAMR TAAAHSAYSG
     LSVLRDLSRH RGTQVLAPVV FTSALGLGEL FSPEVTGQFG TPAWIISQGP QVLLDAQVTE
     FDGGVLVNWD VREGFFPPGV IDAMFAYHID ELLRLASADD AWDAPGPAAL PEAQRAVREA
     INGRTAPPSG EALHDRFFRQ AERQPDAPAV FAGSGDLSYA QLRDQALAVA AALRAAGAGA
     GDTVAVVGPK SAEQIPAVLG ILSVGAAYLP IGADQPRDRA ERILQSGRVR LALVCGGRQL
     SLPVPGLVLA DVLGGAPADA EIACARVDPG ELAYVLFTSG STGEPKGVEV THDAAMNTVE
     FIGRHFEIGP ADRCLALSTL EGDISVMDVF VTLRTGGAIV VVDEAQRRDP DAWARLIDTH
     RVTVLHFMPG WLEMLVEVGR GRLSSVRVVP TGGDWVRPEV VRRLRAEAPG LRFAGLGGAT
     ETPVHNTIFE VTEPIPADWT ALPFGVPLPN NVCRVVGDTG GDCPEWVPGE LWVSGRGIAR
     GYRGRPDLTA QRFVEHDGRT SYRTGDLVRY RPDGTLEFVG RADHRVKISG YRVELGEIES
     ALRRVPGVRT AVAALIAGAG ESDVLAAQVG TDDPALTGEQ VRQYLADLVP AHMIPRHVAV
     VERIGFTAAG KLDRRAVARE LHSVVGQSHS PGHRAASTPL EGALALILGD LLGRDDVGVD
     DDFFALGGDS VLATQAVARI RAWLDAPDVM VADMFANRTV SALAAVLRAA EDDPDRLDHV
     AELYLEVIGM DAESVLTATR QTTKS