ID L8ESW8_STRR1 Unreviewed; 1283 AA.
AC L8ESW8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:QST82666.1};
GN ORFNames=SRIM_023140 {ECO:0000313|EMBL:QST82666.1};
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:QST82666.1, ECO:0000313|Proteomes:UP000011074};
RN [1] {ECO:0000313|EMBL:QST82666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82666.1};
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:QST82666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82666.1};
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:QST82666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82666.1};
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};
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DR EMBL; CP048261; QST82666.1; -; Genomic_DNA.
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; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
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; 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; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
SQ SEQUENCE 1283 AA; 136492 MW; 08E86E227146B078 CRC64;
MVRLRGSLDP AALRAALVDV LDRHESLRTV FPEVDGAPQQ VVRVVDDVPG WQAARTTEEE
LPAAVDRFVD HAFDLTAEIP LRAALFPVAD GEAVLALVLH HIAGDGQSLA PLAADLQVAY
AARAAGTEPS FAPLPVQYAD YTLWQRRVLG DEQDPDSPIS EQVAYWRRAL AGLPEELDLP
FDRPRPAVSS HRGGSVAVHL DAALHGKLAE LARAHDATVF MVVQAALATM LSRLGAGEDV
PIGSPVAGRT DQALDDLVGF FVNTLVMRTD LTGNPSFAEL LHRVRETGLA AYAHQDVPFE
RLVEVLQPAR SMARHPLFQV MLAMENGGPA RPAADWPGVE AEPYSVDNVA AKFDLTFNLA
ESYEPGGEPS GIDGELEYAT DLFEESTARS LADRLTRVLT AVTADPARPV GEIDLLSGPE
TARLLDQGQH IDAGAVPTTF PELFESVVAA DPDAPALVAP ARDGAGRDTL SYGELNARAN
RLARLLIARG AGPEQFVALA LPRGTDLFVA LLAVLKTGAA YLPLDLTYPQ ERIDFILRDT
APRLAVSLAE VSGVLDTAGR SLPVVLLDER EPDLAEQPSH DIGDAERSAA LLPSHAAYTI
YTSGSTGRPK GVVVSHAGIS SLVATHRRWP AAGAGSRVLQ FAAVSFDTSV WEITMGLLTG
AALVVAADDE RGPGEPLVRL LTEQGVTHAT IPPAVLARLD PARLPAGRTV IVAGEASGPG
LVERWAAHHR VINSYGPTET TVDASIAVCA PGPRDTVPIG GPVVNTRLYV LDPSLRLVPP
GVPGVLHVAG AGLARGYGNR PGLTAQRFVA DPYGPPGSRM YNTGDVVRWN ARGELEFVGR
ADDQVKVRGF RIEPGEIETV LAGHPSVEQV KVTVREDVPG DRRVVAYLVG AADTADLREL
AAERLPDYMV PAAFVALPAL PVTSRGKVDV KALPAPAYAS SGGRAPRTPV ERALCEVFAE
ALGVDTVTAD DNFFELGGHS LLVLQVVNGV ERTLGVRLPL RSLFEHPTVA GLAESGLDGG
PGGFEPLLPL RTGGDRAPLF CVHPVGGLGW DYFGLLRGLD PDRPVYALQA DGMDGDGETG
LPDTIEEMAR AYVTRLRDVQ PTGPYHLLGW SFGGLIAHAM ATRLQEDGEE VALLALLDSY
PPVPGAAPST TDQEEEQTAL LEFLGIDPAE FGGTAPTPEE LARLLADDPI TYAALGTERL
LAIGRIIGRG VRASREFRPA VFHGDPVFFR ATEDQAADLR PESWAPYTEG HIEIHPVDCA
HSDMLEQRSA LTKITAVLSE KLT
//
