ID A0A1J5LSJ6_9PROT Unreviewed; 1548 AA.
AC A0A1J5LSJ6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptide synthetase {ECO:0000313|EMBL:OIQ30561.1};
GN ORFNames=BM562_09445 {ECO:0000313|EMBL:OIQ30561.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ30561.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ30561.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ30561.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIQ30561.1}.
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DR EMBL; MPDC01000012; OIQ30561.1; -; Genomic_DNA.
DR STRING; 1860092.BM562_09445; -.
DR Proteomes; UP000183546; Unassembled WGS sequence.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd08700; FMT_C_OzmH_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR024011; Biosynth_lucif-like_mOase_dom.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1433..1509
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1410..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 166748 MW; 604F984C4F34C800 CRC64;
MTEFSTVVIG NQSLLIGCSE ALIARGHHIG AVVSDNSDIL SWAQDAGLAT FATPDAITTE
FDWLFSIANL RVLPDAVIAR ATKGAINFHD GPLPERAGLN TPNWAILEGA KEHGITWHLI
EGGVDEGDIL AQRRFAVAPD ETAFSLNSKC YGAALDSFTE VLEQLESGAL RRLPQDLSHR
RYHARADRPA GGGLLQFDQP VADLVRMVRG LDMGGYWNPL SAAKLDLGTE VALVGAAEAV
VSEQIGQGQV EQAQIGQVLS VDGPSLTVAC TDGAISLSDL KTPSGAPLSR LGQIEPGICL
PLWQVPRISA LEAALRSTQK AEPFWRRQLA EMQPLPVPLT LHMAPPDSAT TDRLETEITL
PDDLPSARLM TIVLACMLRS TGETSGSIGL RLPCLLTAAR PGFISDWVPL NADQDQTLES
VSAHMATVLE RAGTEGGFCE DLMARAPEIP PQDPPAVCLC LDMDIVPQGA PLALLKQGNR
LRLSAHSDHL SETALSYLAA RLSTLLSEAG PHDGSPLHAL PVLPAAERKL MLEDWNATQV
DASAPQTIHQ AFEAQVTRSP EATAVVFEDQ SLTYAQLDAR AHALALHLQK SGVRSGSHVG
VYLRRSLDLV VATLGILKAG GAYVPLDPAY PADRIAHFIR DSQADVILTQ AALLDALPDC
KATVVDLEGL DLSPQPDRGL AGGATSDDLA YLIYTSGSTG LPKGVMVRHR NVINFFTGMD
ACIPHKPGDS WLAVTSLSFD ISVLELFWTL ARGFKLVLSS DESRLQLANG PVALSDRKME
FNLYYWGNDD GAGEKKYDLL LEGAKFADSH GFNAVWTPER HFHAFGGPYP NPSVTGAAVA
AVTQNIAVRA GSCVAPLHHP ARIAEEWAVI DNLTGGRTGI GFASGWQPDD FILRPENTPP
ANKPALFDAI KTVRSLWRGE AVAFPRQDGS LHKVVTQPRP ISPELSVWVT TAGNPDTWRE
AGLAGANVLT HLLGQSIPEV GDKIALYHAA LREAGHDPAD FTVTLMLHSY LAETRAAARE
VARGPMKDYL RSAAGLIKQY AWAFPAFKKP KGAKTPFEMD LGSLSPDELE AILDFAFDRY
FEDSGLFGTV DDAVARVEQL KRIGVDEIAC LIDYGIETQK VLAGLVPLAE VLRETNRRPE
LAADDVSLAA QIVRHGITHM QCTPSMARMI ATDPDAGPVL RQLQHLLVGG EALPGDLVAQ
LQDRTDALIH NMYGPTETTI WSTTETLTTR PGGVAPIGRP IANTSVYVLD PQDHPVPIGA
AGELCIGGAG VTAGYWHRRE LTAERFPADP FRPGSRMYRT GDLVKWTTGE RLEFLGRTDH
QVKIRGQRIE LGEIEAALAG LDGITAAVVV PRKIGTDERL VGYVTSAMPQ PEAIVKARLA
QHLTASMVPS HIVTLDSFPL TPNKKIDRKA LPAPHADRAP VPDGDQVETR PAPLTSEAEH
HIAKVWKHLL GMPDVRPDDN FFALGGHSLL AVQAHRDIRA ALPTAQLSIT DIFRFPTLAG
LARHIEQRLG HTAPVTRPAS VSTPPGIDRS DTMSKRRAMR ATRKARNG
//
