ID B5GIC0_STRSH Unreviewed; 2169 AA.
AC B5GIC0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:EDY46066.3};
GN ORFNames=SSBG_04126 {ECO:0000313|EMBL:EDY46066.3};
OS Streptomyces sp. (strain SPB074).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY46066.3, ECO:0000313|Proteomes:UP000002779};
RN [1] {ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY46066.3, ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain SPB74.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; GG770539; EDY46066.3; -; Genomic_DNA.
DR Proteomes; UP000002779; Unassembled WGS sequence.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound 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 CDD; cd05930; A_NRPS; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
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; PF00668; Condensation; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 794..868
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1861..1936
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2169 AA; 232461 MW; 4A17D90AD6DA5F22 CRC64;
MRRPRSPSRR PATRRPSLSC TRPGCCAPGS PPRSAPYWTW PGSATGRSAG SARRPATRGS
PRSATTTGPP SRPSRRCGRA RAKSSRRSGR RPGSSARTRR TTTCTPCCST PASRRCSRGR
SRRTRTAAAA RTVRAARRGR AGAGAPAPGV RLPLSLGEID LAPSGDRALW AHGTVTRDDG
RELLADLALY DAEDGTPLGR VSGFRAADID QVSTTVSRAT VDSWLALPEW VPLPGLAPRS
DAGNGEEAAA YVGEATTRDG GLPAAATADA PAAASGAAPE PGAEGPRDWL VLADTTGLAD
AFAALVRERG DRCRLVRPGP GYAREETGDV TLAPEDPVHL DRLFAELDGE GAPFRGEVVH
LWNLGLPGLA ESSGADIGTA TARGAWTLVA LARVLRARRD TCRLHVVTRG AQPVAAGDAV
EPLGAPAWGV TRVLRHQELA RHRGKLVDLD PVRATPPDEA AALLAEFLAD DEEEIGLRGN
TRATLRLQPA APRLTGPLPP RLRPDGTYLV TGAFGALGRL LCRTLVRRGA RRLVLLGRTP
LPPRAAWRTT APEGRAGQAI ALVREIEALG ASVVLAPVDL TDEAAFTGWL ATYRAGDPPP
LRGVFHLAGQ VRDTLLADID RAAFDTVHAP KTTGAHLLDK HLRDEPLEHF VLFASVASLL
TTAGQTNYAA GNAFLDALAH RRRAAGLPAL SLDWGPWATG MIEELGLEAH YLHSRGMSSL
SPEAGMSVLE RVLGQDLAQL VVATVVDWRT FLAWYDTPPA LVQDLAASAG DRAAEDEGDL
LAAFRAAGPE ERRALVAERF TRLVATVLRA APEEIDPAGG LGAHGLDSLL AMELRARSQA
ELGVAPPVVA LLSDTPVAEL AARLHEELTE RLAQDTPEGA GTVELWDDDG DFPLTQNQKA
LWFLKQLNPE GHAYNIGGAV EVRAELDPEL MFAAVRRLVA RHPALRTGFH LREGRPVQRI
GDGREPDLGW FDVEGQEWEE IKERIIHEYR AGYDLEQDAL FRFRLFRRGP DRWVIMKAVH
HIVSDAVSTF TFIEELLEVY EALKEGREPA LAPVPARYVD FLNQQNKFLA SPEAARMRDY
WRAHLPAEVP LLDLPTDRPR PAVQTHNGAS EFFVLDETLS ARVHTLAQRH GVTPFMVLLA
TYYVLLHRWS GQDDLVVGSP VTGRTRQEFS SVYGYFVNPL PLHADLSGDP AVEALLGQVR
DTVLGGLDHQ EYPFVLLVDE LGLQHDSSRS AVFQAMFILL THKVATEQYG YRLEYIELPE
EEGQFDLTLS AYEEEAEGRF HCVLKYNTDL FDAATVRRMA AHYTRLLDSL VHAESGTPVS
ALDMLAAHER EELVRETSGA ARAALEPGAV PVHRLFARAA RENPSAVAVR VPGGDALSYG
ALDARSAGLA DRLRALGIGA GSVVGVALPK SPELVVHLLA VLRAGGAYLP LDPALPAGRL
ARVLAGAGAA LLITEGAAPE GLPCRSLAAG ALAAQEPLPA AETADDLDAP AYVIHTSGST
GEPKAVRVAH RNLAAAYASW HREYRLGEEV RVHLQSAQPS FDVFTGDLVR ALCSGGTLVL
AGRDLLLDTA RLYTVLREER VDCAEFVPAL VRGLMDHCVR EGLGLGFLRL LVVGSDTWKV
AEYERLRRLA GPGTRVLNSY GVTEATIDSA FFEGPADGLD PGLAVPVGRP LPHATLHVLD
PHGNPLPAGI TGELWIGGEG VALGYAGRPG LTAERFTERE LLPGAGAERL YRTGDLARWD
TAGRLHLLGR ADSQVKLRGH RIETGEIEAH LAARRGIARA VVAVRPGAGG EDALCAWYVP
EPGAEVSPAG LRRALADALP SYLVPAYLTE VGALPLTAHG KVDVRALPAP SASEARSAYE
APVTLYEVSM AAHWKALLGL EEPGLADDFF ASGGSSIKLI ELLHHLRTEF GVGVPVSRLY
QVTTLHGMAA AVEERVTGTT ADEVPHLTFN PGAERPLFCF PPAGGHGLVY RGLAAALPDH
RLIAFNYLPG DDKVSRYADL VTAAVPKGPV PLLGYSLGGN LAFEVARELE ARGREIAHVV
VLDSRRSLKA YEPGPEVLKA FESELGGHLH QHTGSEIVTA AVMEHAAEYL RFCGRTPNTG
TLAAPVSVLT DEDKADLYEE GVPGSWHGSS AAGHRVLCGF GTHAEMLDAE HLPRNAQLVR
RLLDGQGAA
//
