ID L8EXQ4_STRR1 Unreviewed; 2389 AA.
AC L8EXQ4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:QST82183.1};
GN ORFNames=SRIM_020315 {ECO:0000313|EMBL:QST82183.1};
OS Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS 4667 / NRRL 2234).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST82183.1, ECO:0000313|Proteomes:UP000011074};
RN [1] {ECO:0000313|EMBL:QST82183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QST82183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA Herron P.R.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QST82183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT "Bilateral symmetry of linear streptomycete chromosomes.";
RL bioRxiv 0:0-0(2021).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP048261; QST82183.1; -; Genomic_DNA.
DR RefSeq; WP_003979972.1; NZ_CP048261.1.
DR GeneID; 66856350; -.
DR Proteomes; UP000011074; 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: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; cd17652; A_NRPS_CmdD_like; 1.
DR CDD; cd19543; DCL_NRPS; 1.
DR CDD; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 4.
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; 3.30.559.30; 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; 2.
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; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
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 968..1043
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2030..2104
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2389 AA; 253553 MW; 5D5C66D76D1B80DC CRC64;
MKRSGISDVL PLAPLQKGLL FLSEYDPRSA DAYSLQLSVE LDGPLETGAL RAACAALLGR
HPNLRACFRR RATGDPVQLV PHEVELPWRE LDLPGADAGQ LRAAADEERG RRFDLARPPL
MRFVLVRQAE TRHTFIWTLH HSLADGWSLP MLIQDLFTLY AHGGRADGAG LPQAAPYRNY
LAWLGAQDED AAHAAWRDAL AGLDEPTRLA PVDGRAPVLP DSLTMDVPER LAAGLAARAR
ALGVTLNTVF QAAWSLVLGA LTGREDVVFG TVTAGRPAEL PGVEAMVGLF ANTIPVRVTA
RPGQSVAALL ADVQERQSGL MPYEHIGLAD IQRQAGIGEL FDTVMLFQSY PMDEDQLAAS
LPGLRVADAA IRSVTHYPLA LAVLPGPGTR LGLRFDYAPD LYGPADAERF GRRLLRVLEA
IAADPEQPLA RISVLEPVEA RLLQEAGDAV ATAAPARPVA EAVEERVREL PDDTAVVCGD
DTLTYRELNA RANRLAHALV AHGAGPGRTV AIALPRSTGL VVAALAVLKS GAAYLPVDPD
HPAERNTVVL EDTRPVLALT TTATDGKLPD AGQTRWIMDL PDTAELVAGF PDTDLTDADR
ARPITADDAA YVLFTSGSTG RPKGVVVTRG GFANVIEDIR HRYALERGET LLSVTTFGFD
IANTELFGPL VSGARLALAD RETVRDPAAL GRAVTATGAT VLQATPSLWQ ALATVAPDVL
GGVRGFVGGE ALSEPLGETL RKATASITNL YGPTETTIWS TGAPPLDGVR AGAPAIGFPF
ANTRLHILDD WLRPVAPGVI GELYIAGAGL ARGYLGRPGL TAERFVADPA DPAGGRMYRT
GDLVRLGADG QVEYVGRADH QVKIRGFRIE LGEIENALSG HPEIGQAVVA VREARPGEPL
LAGYLVPADG AAVPEPGALR AYLAERVPEY MVPAAFVTLD ALPLTPNGKV DRKVLPDPEL
RSRATGRAVR SPQEDLLCQV FAEVLGLPRF GPEEDFFAHG GHSLLAARVV SRIRTVLGAE
VPVRALFEAP TPAGLAERLP RAGAGAARPA LRPGDRPEDV PLSYAQLRLW FLNRLDGAHG
TYNISLALRL TGDLDRDALG GALSDLVGRH ESLRTVFPDR DGTPRQHVLP LDEAGFGLRE
HVTDEERLDG LLASEAARGF DLAREIPLRA DLFRLSATEH VLLLVLHHIA GDGWSLTPLA
DDLARAYAAR RGGTAPEWAE LPVQYADYAL WQREVLGEED DADSLAARQL AYWKTALAGL
PEEIELPADF ARPAVAGHEG AEHTAFIGPD LHRALAGLAR AHGVSLFMVV QAALAALLTR
MGAGEDIPLG SPIAGRTDEA LDDLVGFFTN TLVLRTDTSD DPAFTELLRR VRETDLAAYE
NQELPFERLV EVCNPVRSLA RQPLFQVMLA FQNTAEAKAA LPGLTAAVHP VGSATAKFDL
AFQLTERAAG DAAADGEPGG IDLVVEYSTQ LFRPETVRQL AERFTRVLAS VAAAPKAPLS
SIDVLGDAER RRIVGEWNSA TTEVPERTVA QLFEEHAARQ PDHEAVVFGE VSLTYGELNA
RANRLARVLA GRGAGPGTLV GLLLPRSVEM IVSILAVLKS GAAYLPLDPD YPADRIAYMV
GDAAPVCVLA VPGTGGALRD GGTEVIELDG GVGGDARPAT DLTDADRTRP LTCRDAAYVI
YTSGSTGRPK GVVIEHAGVA ALAADHVRRF GLGARSRVLQ FASPSFDAAT AELTMALLSG
GTLVLATPES RGPGEPLADL ISRHGVNLAV LPPVVLAAFP EDITLPGELT LITAGEALPP
EVAARWADGR TLHNCYGPTE STVCATSSDP LTGEGKPPIG RPLANTRAYV LDGRLNPVAP
GVTGELYLAG AQLARGYLGR PGLTAGRFVA DPFGPAGARM YRTGDLARWT ADGTLEYAGR
VDHQVKLRGF RIELGEIESA LAAHPGVAQA VAAVREDRPG DRRLAAYVVP EGAPVPAAAL
REHLSGLLPD YMVPGAFVTL DALPLTPNGK VDRKGLPALD APEAAAHGRT PRTERETLLC
QVFAEVLNLP EVGAEADFFE LGGDSIRSVQ VVGRARKAGL DLALPDVFRH KTVEALAAAL
ERAERAAGTT FLDRVRQRLD DPSADAPLDP YGPVLPLRTT GDLPPLFCVH GGMGFALPYL
GLAGHIGERH PVYGLQASGL TGTGPLPGSI AEVAAEYVER LREIQPAGPY HLLGWSYGGI
VAHEMAAQLE AAGEEVALLA NLDSYPAEPG EPAPTDAELL TAVLEYCGLE TAANDDGGPT
PETVRDALRR ADSPLGDLDI PRLVDVMRNH VRLVQEHTPG RVRTPVHLFV AELGLPPEER
AARPGRWAAH TDGGTAVHPV PCGHEFMMHS GPQAAIGQAV ADELALLHP
//