ID B2HM87_MYCMM Unreviewed; 1670 AA.
AC B2HM87;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Non-ribosomal peptide synthetase MbtE {ECO:0000313|EMBL:ACC42107.1};
GN Name=mbtE {ECO:0000313|EMBL:ACC42107.1};
GN OrderedLocusNames=MMAR_3691 {ECO:0000313|EMBL:ACC42107.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42107.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC42107.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP000854; ACC42107.1; -; Genomic_DNA.
DR RefSeq; WP_012395307.1; NC_010612.1.
DR STRING; 216594.MMAR_3691; -.
DR KEGG; mmi:MMAR_3691; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_61_1_11; -.
DR OrthoDB; 2472181at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 CDD; cd05930; A_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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_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:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 984..1059
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1554..1628
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1670 AA; 182222 MW; B7CDEC1D0A0BA2B5 CRC64;
MADDVRTLQD RRRELLRRRI AESGLAAEQS SDQPGICPGE RYRLSDGQRR MWFLQTMDPD
DVTLNICVAY RLAGLVDEDR LHTAVNDVVA RHAILRTTYG VDTEGEPYQV FSDDVEVGWR
REDLTRLPEA GHERQIESLA ADEFGRPFDL TNELPLRITV IRTRADELVL LLVVHHICWD
DDSWEVFFGE LSAAYNDLPI NDPAAQFLSV EVLQNSAAPS VADVGYWAET LRPLPEPPEL
PGVSGANPCR RAQRRVRPLP AGLFSRVEDF ARKCSASPFM VLLAAYGVLV RRYTGASDFL
VSVPVTERSG AAAGALGYFG NTLLLRITTR SQDTFTSFVN EVRETCLAGF AHQSVGIDRV
VREANPERMG RDGMDLLVRL GFNMRKSAGG LALDGVVVRQ LGLGAVAAHL PLSLTIALDP
DDVSVEFEYQ QQLSSVLVDQ MLVHYLQLVD KALAEPERPL SSLDILGAGE RDSVLAQSHG
ELVEMPATTM VKLLEATASA AGTATALALV SDEAELTYSE LHRRANRLAR WFIGQGFGPE
DIIGLRMANS IEFIVAMLAV LKAGAAYLPI DPAYPDERID YLITDARPQT VIGRPELDVA
ERAAADNSDL PLSDSDRLRP LRPGHLAYVI YTSGSTGRPK GVAVSHHAIA EHVQGFVAEW
TMTAEDRWLQ FSSVSFDASL ADIFVTLFLG AQLIVPKPDA FGDISYVADL ISRRGVTVLH
LVPSMLSTLL LLPQVQQWRQ LRHVPVGGEA LPGEVADRFA GYFDAELRNH YGPTEAVVCS
THMVVTGSHG ARVVPIGVPN RNVYAYVLDE QLHPVPDQVI GELYLGGSQL ARGYLGRPTL
TAQRFIADPF NPGMRLYRTG DLVRRNHCGE LEFVGRADEQ VKIRGFRIEL GEVESVITTH
PAVRHCLVVA EETEAGPMLA AYLVPAAAQV DLEEIRAHTA AAVPEYMVPG AFAVIPEIPM
TVSGKLDRRA LPAPTPIATR RYREPETATE RWICSIFAQL FGRQRVGAED SFFGLGGHSL
LAARLVAQIR AEFGVDLTVR TIFDAPTPAG LAARLVERFR NDFELDLDNL AADDMPLDPK
RARPGFVKSA RPQRLPLSHS QLAAWFQYRI EGAREEFNMP LALRFEGPLD SVALAAALND
VVARHEALRT NFDEHEGVPY QIVHPSRTVQ LAVRAIDQDE FDDVSTQLRR HVFTPESGPL
LQANLLVLGP DTHVLLLIVH HIVSDHASLE IVFDDLIVAY RARLQHNAPQ WDILPIQFAD
YAVWQRNTFE SNWGQTELDY WRDALAGLPD EISVATDRAR PRVLGKRGEV VQFSVPAARR
AALTQLAERN GATEFMLYQA ALAVVLHKLG GGTDIALGSP VAARVEPATA QLVGLFANVV
VLRTDLSGDP TLRSILVGSR DTVLDALAHQ ELPIERLVEA LNPPRALSRN PLFQNMLNFR
GEDWALVPRD LTGRGETTVV PLPVNFEVAL LFLAIGMSVT PSGELDVQVI ANADLYEPAT
VALIADALDA ALAAFATTPD LPLSAVQLLP SADLAKLLAP PLPAGPAASP PVAAGSAETE
RRLTAMLEEL LEITGIDRDE NYFALGGDSI IAIKWSAQAG ALGLPFPPAM VFEHMTIAEL
AAAVDAANGE PVVEADPPPA QEYTPMSASG LAPDALAKLS ASWLQQGSAS
//