ID A0A2P8DKU5_9ACTN Unreviewed; 1534 AA.
AC A0A2P8DKU5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Phosphopantetheine binding protein {ECO:0000313|EMBL:PSK97844.1};
GN ORFNames=CLV63_107240 {ECO:0000313|EMBL:PSK97844.1};
OS Murinocardiopsis flavida.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Murinocardiopsis.
OX NCBI_TaxID=645275 {ECO:0000313|EMBL:PSK97844.1, ECO:0000313|Proteomes:UP000240542};
RN [1] {ECO:0000313|EMBL:PSK97844.1, ECO:0000313|Proteomes:UP000240542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45312 {ECO:0000313|EMBL:PSK97844.1,
RC ECO:0000313|Proteomes:UP000240542};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSK97844.1}.
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DR EMBL; PYGA01000007; PSK97844.1; -; Genomic_DNA.
DR Proteomes; UP000240542; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041618; PKS_DE.
DR InterPro; IPR013968; PKS_KR.
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 InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000240542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1154..1229
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1534 AA; 158597 MW; EB34823C7EB95052 CRC64;
MLPRSLHVGE PSSHVAWAGG GVRLLREEVA WTKAQGEGVR RAGVSSFGVS GTNAHLIVEE
APEEVPVEVP VSVGGASEGS APVSGDGSGA GPVVVAWDRL SAVSGQESAP ISGETSVLMP
VPVVVSGASG AGLEATAARW AGFLRDQDQG NRQNRQDRAD GSGVSVVDVG VTAGAGRAGL
EHRAVVLARD TAELAGLLEE VAAGREPSGV VRGTASAGAG AGSGASAGAQ VVFAFPGQGT
QWVGMGARLL AESPVFAARM AECAAALGPF VDFDVLAVAR GDADAASLER VEVVQPVSWA
VMVALAALWE AVGVRPSAVV GHSQGEVAAA CVAGVLSLAD GARVVAERSR IIAGSLAGAG
AMAAVALSPE QVQERLDADA AAAGSDAGAD PAWGGVSVAA VNGPSSVVVS GDTTAVENLV
REWSAEGVRV RRIAVDYASH SVQVEQVREE LIAALEPIVP GAGRVPFYST VRGEVVAGTE
LGAQYWYWNL RLPVGFAGVV EQLVSEGRGV VVEVSAHPVL GVGVQELVEA AGGAVVGSLR
RGEGGLDRFL ESVGRVFVCG VGVDWPAVFT GSGGQSAAGL PTYAFQRQRY WLNPAPAPVG
VDHFWQSVSA EEPDELAARM GVDPAAVRVV LPALEKMREQ DRERSLADEW RYKLTWRPVH
GRKAGDLVGR WLVLVPEGLA EDKAARAIMD GLQALDGVPV QILPVAADSR EGLAEAIRTA
ADGDGDQAEV AGVVSLLALD DDPHPVHPGM SQGMAATILA VQALADAAVS APFWLVTRCG
VVVEEAHEPV SPEQSALWGL GAVLALDQPR SWGGLIDMPA DPDGSDVGEL VAALSQPGED
QVAIRRGATW ARRLERAPVG AAGPPQGEWR PHGTVLVTGG TGGVGANVAR WLAREGAEHL
VLVSRSGSAA AGVQELVAEL TASGARVSVV ACDVADRGAL RDAVAGVAEW SELTGVLHAA
GVGHDGVPLG ETTLAEFSAA TRAKVMGAAN LAELLADHPL DVFLMFSSGA AVWGQGGMAP
YAAANAYLDG LVWQRRANGL NGSAIAWGAW GGGGMVDAFG AEQMAKFGIR VMPPEPLTTL
IGQVVAGGES HLVVADIDWR RFAPVFAMAR PRPLMTGIAD YTRALTESEP SDDASAAAAF
RTALAEMSEP DRVDELTRVI RESAARVLGH TTPDSMGAGQ HFLEAGFDSL TAMELRNKLN
ATTGVQVPTT AVFDHATPAE LARHLAAEFV AGKRALAGGA EAPEAPTSGE TLSDLLRGAI
ASGKIHEGLD VLEVTAKLRP SFAGPEEVVS PTEPVRLASG PNLPRLYCFS TPMVLGGAAQ
FARLATHFQG VRDVYALPVP GFGPDEALPE TVDAVVRTWA QTITATDEPF ALLGYCAGGM
FAHAAATLLE EAGTPPSGLV LLDVFLPETS IIDDLGYQLV EGMFAREESF GPFTSARLAA
MGRYYRLFQQ MRLGDTAAPV LFIRPDTPLP SGPEGIRSRE GNWRSSWAEA HDLREVRGDH
LSMLEGESAS MAGAIEPWLS GLARHPEGRG DGAR
//
