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Database: UniProt
Entry: A0A1X2LNU7_9MYCO
LinkDB: A0A1X2LNU7_9MYCO
Original site: A0A1X2LNU7_9MYCO 
ID   A0A1X2LNU7_9MYCO        Unreviewed;      1069 AA.
AC   A0A1X2LNU7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE   Flags: Fragment;
GN   ORFNames=B8W66_23155 {ECO:0000313|EMBL:OSC36234.1};
OS   Mycobacterium decipiens.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC36234.1, ECO:0000313|Proteomes:UP000193247};
RN   [1] {ECO:0000313|EMBL:OSC36234.1, ECO:0000313|Proteomes:UP000193247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC36234.1,
RC   ECO:0000313|Proteomes:UP000193247};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (APR-2017) 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:OSC36234.1}.
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DR   EMBL; NCXP01000060; OSC36234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2LNU7; -.
DR   STRING; 1430326.B8W66_23155; -.
DR   Proteomes; UP000193247; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   CDD; cd08952; KR_1_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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; 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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1015..1069
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   NON_TER         1069
FT                   /evidence="ECO:0000313|EMBL:OSC36234.1"
SQ   SEQUENCE   1069 AA;  115419 MW;  3BC3BA2F0AA8078F CRC64;
     MPPLLVWAIS ARSPRALCAQ AQRLHEHLIS HPDVDLTDVA YSLATTRSHH PYRAVITSHR
     GTENARDHLL EVLQALGADQ PHPQLTSHHH LPHLAGKIVF VFPGQGAQYP GMVAQLYDNH
     HVFAAALDEC DQALRPWTGW SVRDVVCQDP GAPRLDRADV VQPVLFAVMV SLAKTLGSYG
     IVPDMVIGHS QGEIAAAYVA GVFCLADAAK IVALRSAALA RLSGAGAMAS VLLPAHQLRS
     RLQRYGDALS IAAVNGPSHT IISGQPSAVE QFSAACDQDG IHTRRVAVDY ASHSSQVEQL
     REHLLDELAG LTPNPAQMQL YSTVHSALSD QPLDTTVMNA DYWYRNLREP VRLHDSVEHL
     LATGEHTFVE LSPHPVLAPP IADTLARTSG RTQSAVITTL HRDHPDLDML AGTIAQLHAH
     GHSPSWQSLY PHAQAVALPT YPFQHRSYWL APTPTADIGL PGEEVLWNAI EDDAVDTVAK
     VLKISDAKDL TLEPVVHALR QWRKDLGVRS MINGLRYRVG WQTITPNTFP RTRQRLLVLA
     FPEQADDNAW IASLSAQYTD NLEVLAIDPS DFDKNSLTAL LSDTVARTGC EDIVSFMALA
     QRPHPGLSGI STGLIATLRV GQAYGDSGLD VPLWVLTQGG VATSPDENST VSPSQAAVWG
     LGQSICIEYP DRWGGLIDLP DIATARNVEH LHKILTCPQS EDQLAIRQHG ISARRLYEAP
     LPLDRLDRAT TWTTSGTALV TGATGRLGKH VARWLAEAGA SHLILLSRHA AQSPQTAELE
     QQLDAIGVGA TLVSVDVTDR EALATVLADT RNQHGPIKTV VHAAATIGWH TISEITTEEF
     CQDYAKAVGA DNLTELLDDE PPATFILFSS AAGVWGGAQQ GAYAAANAHI DALASQLRAN
     KHTTAISVAF GLWADHAGMP DEALNSFQRI GIKALSPETA LAALQQSLET NDTLITIADV
     SWNQFLPAFT ARRAHPLLTE LASAHAPTTT NTTKNAHSEA FTARLTTQTA DQQLRTLTDL
     VTRTTATVLA HPDPTTLDTD RPFKDLGIDS LSAVELRNTL ARHTGLTLA
//
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