ID   A0A075R5E8_BRELA        Unreviewed;      1075 AA.
AC   A0A075R5E8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=NRPS domain-containing protein {ECO:0000313|EMBL:AIG26696.1};
GN   ORFNames=BRLA_c023760 {ECO:0000313|EMBL:AIG26696.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG26696.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG26696.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG26696.1,
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   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP007806; AIG26696.1; -; Genomic_DNA.
DR   RefSeq; WP_003337613.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075R5E8; -.
DR   STRING; 1042163.BRLA_c023760; -.
DR   KEGG; blr:BRLA_c023760; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_2_10_9; -.
DR   Proteomes; UP000005850; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd19534; E_NRPS; 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   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; 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; IPR010060; NRPS_synth.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 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   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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          515..589
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1075 AA;  122503 MW;  E26AB95DD04A9265 CRC64;
     MIHSHSLTTP YLSDKTIHQL FESQAEKNPD NPAIILEQEK LTYQELNSKA NQLARLLIEK
     GVQTDQIVGI FMDRSIEMVI SILAILKAGG AYVPIDVEYP QERIQYMLKD SQTKIVLTQH
     ALVGLIREAD FQGQVITFED PAIMMQAELN LNLDCKNTDL AYVIYTSGTT GSPKGTMLEH
     KGIVNLIDYF QKILEITPND RVGQFASISF DASVSEFFMA LLTGASLYMI SKDTINDFVS
     FETFMNQHKI SIITLPPTYL IHLNPERILY LRKLITAGSA TSFPLVNKWK DRVTYMNAYG
     PTESSICAST WIAKTEDAGQ QAVPIGSPIQ NTQIYILNPN LEEVPFGETG ELCISGIGLA
     RGYWNRPELT SEKFITHPYL PGEKMYKTGD LAKWRSDGTI EYIGRMDHQV KIRGHRVELG
     EVETVLLRYH KIREAAVIAK KDELEQAYLC AYFVETEQVS PAELREHVAK DLPVYMIPSY
     FVRLDKMPLT PNDKIDRKAL PEPHASLLDT TEFEAPTTEI EAILAEIWQS VLGNNRVGIH
     DNFYALGGDS IKAIQVAARL YAYQLKLETK DLLKHPTITE IVPLLKQTSK KSEQGIVEGE
     VGLTPIQQWF FDQQFTNMHH YNQSYVLSHP NGIDEVLIRK VFDKMIEHHD ALRMVYKRVN
     GRIKQINRGK TGPLYDFFTF DLRSNQDVQQ AIYEESYRLH SQINLNEGPL VKLGLFHTQK
     GDHLFIAIHH LIVDGISWRI LFEDISTAYA QVLESKEIAL PEKTDSFQEW SLEIEKYATS
     KELLHEIPYW QALESIAKPT PLPKDFENSL VKQNSIQHMK MELSVEDTGH LLKNVNHAYQ
     TEINDILLSG LSLALLEWAK VDQILINVEG HGREDIIEQA NIARTVGWFT CQYPVLVKMD
     KSDDLSYHIK SVKENLRKIP NKGIGYEILK YKTAKEINTS LSFSLQPSIT FNYLGQFDSD
     LEGQGFTRSP YSQGNSLGAD GKNNISPEME SNMVLHITGV IEKGRMNLSF SYSDQQYKEE
     SIKQLGDKYK YHLLRLIRHC MEKEETERTP SDFSIKGLEL EDVDDIFGLL EESMK
//