ID A0A495JBN6_9ACTN Unreviewed; 1893 AA.
AC A0A495JBN6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RKR86141.1};
GN ORFNames=BDK92_0363 {ECO:0000313|EMBL:RKR86141.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR86141.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR86141.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR86141.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKR86141.1}.
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DR EMBL; RBKT01000001; RKR86141.1; -; Genomic_DNA.
DR Proteomes; UP000277671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0043604; P:amide 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: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; cd19531; LCL_NRPS-like; 1.
DR CDD; cd06173; MFS_MefA_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 Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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; 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; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
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; PF07690; MFS_1; 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; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000277671};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1464..1485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1497..1518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1524..1544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1556..1582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1588..1609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1642..1668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1674..1694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1706..1722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1763..1786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1817..1835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1004..1086
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1862..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1893 AA; 202396 MW; D9E0DAA7F230BF93 CRC64;
MTEVELPARP AATGPPTIPR RPDGRAPLSF GQERLWFMEQ FAPGTAAYVI PVTLRLRGPL
DPDLLGRALD AVAARHDSLR MRFTQDVDGL PAVDLAGPVT VPLVTAHAHS AGRARELVAD
AARQPFDLAT APLLRALLIR LGETDHVLHL AAHHIVTDGW SFDLLLGELA TQYAGYLDGR
PEPSAPAVRY GDYAAWQRER VDSPAVRGQL DYWRGALADV PPLELPTDRP RPAEQGHEGA
THRFTLDAGL TDELRRLGRR HRATLYMTLL AGLQTLLFRQ SGQRDFAVGS PVAGRVVPEL
EHLIGLFINT LALRADLNLD AAAATGAGGS TGSAVEPSFA TLLGRTRTTV IRALARQEVP
FERLVQELHV PRDVSRAPVF QVMFALQNYA RGANRWPAGL VAESFGTGIS SARYDLAVYL
SEADDGLRGS VLYNTDLFDP QTMTRFTDHY RNLLRAAVAR PDLPLVDLDL LDRAERDRVL
SFGAPAPARR AAGATTATSD AGTLADLITP YAVSTSTTAA VVCGGDSVTY RELDHRANRI
ARFLRRRGVG PESLVGVCLE QSVELAVTLL GVLRAGGAYV PLDPEQPPAR LAGMLADAGP
AIVLTDTTLR AQLAPLTDAP LVCLDLVRDE VAAEPETAPP DGASPDNLAY VIYTSGSTGT
PKGVAVAHRQ VLRYLNGIAD RLDVPPAGRY ALLQSMSFDF SVTVFYLALA TGGTVHLVPR
RCTGAELADE LRRHRIDYLK MTPSHLAALA ADVPPGALLP HRALLLGGEP ADPGWAAGLA
EGNTRVVNHY GPTEATVGVT TYRIRATGTG PGPVPIGTPL PYARVHLLDH RLRPVPVGTV
GEIYLGGDRL ARGYLNQPGQ TAGRFVADPF GPPGGRLYRT GDLGRWRGDG ELVFLGRRDH
QVKLRGYRVE LGEVEAALRE HDGVVQAAVL LRDDRLVAYL ERRSGAVTTE PATLRRTLAD
RLPEYMIPTR YVWLDRLPLQ EHGKVDRGAL PPPGDDRPTG TRVAPDGPVE TVIAAVWQAV
LGIDRIGVTD DFFDLGGHSL LATRVVARLR RELPETVDGP VHPVTVMDLF KHRTVRELAE
LAELVTGDGG RAGGLLHELT PPVPATTERV RSLVCVPYGG GSAVVYQPLA DALPVGHRLY
AVAVPGHDIG LADDPRPIPE VARAVADEIL ATVDGPLALY GHCGPGGALA VEIARLLEAA
GRDLDALYLG GVFPFARPVG GVLGPLLRLR LAERIRSDRI YRTWLQAQGA DLGALDPDQA
AFLIRAMRHD ARVAEDYFTA LVHQRVAPLR APIVCVVGDR DRGTEYAEER FREWHFLSDR
TALAVVDEGG HYFLKYRAAE LAEIVTTVDR RLDRPDPATA GANETPAAHV PAEPDPGWRL
TGVSRRTAAE TSTMDGASGA GTAPESTRGG APLPVVADAT VPRTPEPSIR RFALVAVGQI
VTMTGTALTN FALPLWIYLE TGSLARFALF AVLGLVPGLL VAPLAGALID RTSRRRIILL
ACCAAGGAKL VIAAALLADL AQVWHFYLLV AWLSVALAFQ RLAFVSAVPQ LVPKRYLGHA
NGVTQTATGL TQFMVPLIAV ALLEAVDLHG ILVIDVVLYG LAIVVLLAIR FPATMALRRR
ESIGAEITGG LRYSWRRREF RAMLVFFALL NLFLFPALFL LSPLVLGFAD LAEVARIALV
GGLGGAAGGL VMLVWGGPRH HRMRTVLIGT VLLGLACVVT GLRPDLTVIA AGAFGMYLAL
GVVNGVYATV VQTKVPQLFH GRVFALNQMV AWSTLPLGWG VIAPLASGWA EPLLQPGGAL
APTVGAVIGV GPGRGIGLLY VAFGLCIGLT AVVSLRTRVL ARFDDEVPDA PPDDVLGIEA
RQARAARAGT GPTDRSEREV AGAATGTRHA DGS
//
