ID A0A075QY58_BRELA Unreviewed; 641 AA.
AC A0A075QY58;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=NRPS domain-containing protein {ECO:0000313|EMBL:AIG25287.1};
GN ORFNames=BRLA_c009460 {ECO:0000313|EMBL:AIG25287.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG25287.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG25287.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG25287.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP007806; AIG25287.1; -; Genomic_DNA.
DR RefSeq; WP_003335206.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075QY58; -.
DR STRING; 1042163.BRLA_c009460; -.
DR KEGG; blr:BRLA_c009460; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_12_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020459; AMP-binding.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
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; PF00550; PP-binding; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850}.
FT DOMAIN 540..615
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 641 AA; 72931 MW; 26E8F52458EBD1A9 CRC64;
MDLSTLNFLG ETEKHKLLNQ FNDTDANFPQ EMTIHGLFEK QVQERPNQTA VIFNEQSMTY
KEMNERANQV AHSLRKHGVA PDEIVGILAD RNMDMLISIL GVLKAGAAYM PIDPTYPTER
ILYMIHDSQT KIVLAEHREM VPEGCNAELI LLHDSSLLNE ETSDLEHVNK PEDLAYIIYT
SGSTGKPKGV MIEHRNVIRL LFNDRNLFDF TSDDVWTVFH SFCFDFSVWE MYGALLYGGK
IVLVSFEIAR DPQAFRDLLQ EQKVTILNQT PTAFYQLSSE EMQHSDSNLS IRKIIFGGEA
LTPSQLKAWK QKYPNTALIN MYGITETTVH VTYKEFQLHD MDSTVSNIGK PIPTLRTYVL
DSKRNLAPIG VKGELYVSGK GVARGYLNKP ELTEERFMDN PFVSEERMYR TGDLARWLPE
GELEYLGRID HQVKIRGYRI ELGEIEAELL KQKGIKEAVV LVTNDKDAQP QLHAYLTSTE
DLAAGDLRNQ LTTTLPSYMI PAHFIFVSQM PVTPNGKIDK ESLRKIEPSL QESPTEAYVA
PQTPTEKQLV HIWEENIGMQ PISIDDNYFA LGGDSIKAIK LLHAINKEFQ ISFQIGDLYK
HGTIREMGQQ IGEQGKQSSN QKLLKLQELD RLKEKILGSE K
//
