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Database: UniProt
Entry: D6ZBC8_SEGRD
LinkDB: D6ZBC8_SEGRD
Original site: D6ZBC8_SEGRD 
ID   D6ZBC8_SEGRD            Unreviewed;      1164 AA.
AC   D6ZBC8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743};
DE   AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440};
GN   OrderedLocusNames=Srot_2436 {ECO:0000313|EMBL:ADG98880.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS   44985 / JCM 13578).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG98880.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG98880.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA   Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA   Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MbtB subfamily. {ECO:0000256|ARBA:ARBA00007380}.
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DR   EMBL; CP001958; ADG98880.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6ZBC8; -.
DR   STRING; 640132.Srot_2436; -.
DR   KEGG; srt:Srot_2436; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_2_4_11; -.
DR   OrthoDB; 2472181at2; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   CDD; cd19535; Cyc_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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_com.
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   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
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; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN          2..78
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1067..1142
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1164 AA;  124735 MW;  93B92FBDE838C41A CRC64;
     MSEPVISLEK IRHQVAGVLA VPPDSLATDA DLISLGLDSI RMMSLAGAWR KQGVDVAFGA
     LAAAPTLAGW HALLQNAPKK PSPAVRSSAA PVQAGELASA GKVFPLAAMQ HAQWVGRDGG
     QRLGGVAAHL YVEFDGAHVD PARLKAAVDL LVQRHPMLRV QILPEGAQRV LPAAGGQVFA
     HEDLGALAEH DAQERLELIR EQKSHQHLAV HEGQVFDVLL VSLPDGRSRL CLDVDMIAAD
     AMSYRVLVAD LAALYRGERL EPLSITFQEH LERKRAVADS REETDRAWWA ERLAALPPPP
     ELPVLPEAES GLAHSPRATR RHYWLSPQRK QALFERCRSR GVTPAMALAS IFATAIGNWS
     ANPKFLLNLP LFTRDAADSR LDRVVGDFTS SVMLSVDLAE PQTVGERACS LQQSFHEAAA
     HSAYSGLNVL RDLSRLHGEQ ILAPVVYTSA IGLGELFAQG VAETFGKPVH VLSQGPQVAL
     DAQVTEIDGG LLLNWDVREP LLRPGVVEAM FAWYTAEIER LATDPEQWAA LSGQGALPAR
     QREVREALRA SAPASDTQRA LHTGFFENAE RNPGAVAVIA EDGSVTTYAE LRRQALAVAG
     ALAELGVRRG EAVAVALAKG AAQIPVLLGV LASGGVYVPV GVDQPQARRQ QIARTARIAA
     VIAPDDVAAA SVEAWAGTVP AVSATSATEH PRPLPEPVAV TADDLAYVLF TSGSTGEPKG
     VELRHGAPMN TIAAVVDRFG ITETDRCLSL SPLECDWSVF DIFGMFSVGG SVVVIEEASR
     QEPALWAQLM RTHEVTYIGW MPGWLDLLLD ASSGDLPSLR VALAGGDWVS ADLPRRLRVR
     APQTRFAGLG GATETAIHST VFEVPNEEGS PPAHWRAIPF GRPLAGVRCR VVNPRGEDCP
     DWVPGEYWVG GAGIAEGYRG DPERTEQRFV QYQGERWYRT GDLVRCWPDG VLEFVGRMDH
     RIKVRGYGVE LGEVETALRR IPGVARAVVV PLEGVTTRLV GAVSVEAGAD LDANSVRAAL
     GCALPAHMVP DTVVLLEAMP LTAVGKLDRA AVRKLVETAA QAQEGVSPRT SLEAALVRIL
     GEVVGGEIGV LDDFFSFGVD SILAIKAVSQ IRDWLDSPQA AVADFFAART VAGLAERLQA
     KEAEPGRLEK VAEVYLEVAA MPMP
//
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