ID L7ER40_9ACTN Unreviewed; 373 AA.
AC L7ER40;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:ELP61374.1};
GN ORFNames=STRTUCAR8_05644 {ECO:0000313|EMBL:ELP61374.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP61374.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP61374.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP61374.1,
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:ELP61374.1}.
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DR EMBL; AEJB01000688; ELP61374.1; -; Genomic_DNA.
DR RefSeq; WP_006383759.1; NZ_AEJB01000688.1.
DR AlphaFoldDB; L7ER40; -.
DR STRING; 85558.T45_01313; -.
DR PATRIC; fig|698760.3.peg.9668; -.
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 373 AA; 42855 MW; 67E857F5C5A37A66 CRC64;
MSLTLRTISR EQHLAYIQSL PSASHMQVPA WADVKAEWRS ENLGWFDDRT GELVGAGLVL
YRQLPKIKRY LAYLPEGPVI NWFAPNLDDW IQPMLAHLKQ QGAFSVKMGP PVIIRRWEAT
SIKAGIQSPD VKRLRDIEAD FIEPRAFEVA DKLRRMGWQQ GEDGGAGFGD VQPRYVYQVP
LANRSLEEVH ANFNQLWRRN IKKAEKAGVE VVQGGYNDLE EWQRLYEITA VRDHFRPRPL
SYFQRMWTAL NTEDPNRMRL YFARHNGVNL SAATMLIVGG HVWYSYGASD NIGREVRPSN
AMQWRMLRDA YALGATAYDL RGISDSLDET DHLFGLIQFK VGTGGQAAEY LGEWDFPLNK
LLHKALDIYM SRR
//
