ID L7FC84_9ACTN Unreviewed; 381 AA.
AC L7FC84;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:ELP68754.1};
GN ORFNames=STRTUCAR8_05159 {ECO:0000313|EMBL:ELP68754.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP68754.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP68754.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP68754.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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:ELP68754.1}.
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DR EMBL; AEJB01000203; ELP68754.1; -; Genomic_DNA.
DR RefSeq; WP_006376076.1; NZ_AEJB01000203.1.
DR AlphaFoldDB; L7FC84; -.
DR STRING; 85558.T45_00916; -.
DR PATRIC; fig|698760.3.peg.2539; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931}.
SQ SEQUENCE 381 AA; 42678 MW; 2BF57E4ADFFE2C41 CRC64;
MSSLYVREIT REEHLAHLRL SPEASHLQIP EWGGVKPDWL PESVGWFEDE AMPVGGAMVA
AALVLYRPLP GTRRYLAYLP DGPAIDWRAP RLERWLDPLV AHLERIGAFS VRIGPPLVVR
HWDAATVTAG LADPGVRHLH DLPAAEIDGR ALDAGERLRR LGWRPCAEDD GSGFGLGQPR
YGCRIPLAGR TVDDLREALA PHWEQSLVTS ERAGVRVLWG SDADLPDFHR LYTATAAHDG
FKARPPDYFR RMWRALNEED HDRLRLYLAE CDSQVLSGAL MISVGSRVWH SYAASGRLGR
ELRPSSALLW RMLCDARAAG AETYDLRSIT PALTEDRLLG RLRFKTGAGG RPVEYLGEWE
LPVGSQGRML QRALRVYLGR R
//
