ID A0A0M5KVB6_9MICC Unreviewed; 335 AA.
AC A0A0M5KVB6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:ALE05110.1};
GN ORFNames=AL755_05785 {ECO:0000313|EMBL:ALE05110.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05110.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE05110.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05110.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012479; ALE05110.1; -; Genomic_DNA.
DR RefSeq; WP_054010190.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M5KVB6; -.
DR STRING; 1704044.AL755_05785; -.
DR KEGG; are:AL755_05785; -.
DR PATRIC; fig|1704044.3.peg.369; -.
DR OrthoDB; 9785911at2; -.
DR Proteomes; UP000060433; Chromosome.
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:UP000060433}.
SQ SEQUENCE 335 AA; 36817 MW; 07AC61A7C53FFDC2 CRC64;
MTLSVLPCPV RDEWDAAVNS QQGHPMQLWG WGETKAAHNW RVDRVLVKDA DGTLVGSAQI
LLRALPFPFR SLAYLARGPQ AVPGREIDVL DAVARYVKAT HKSVALSIEP DWDADTVASA
SLPAAGWQRS ASTILIPRTL ILDLSRSEDE LLAPMAKKTR QYIRKSGREA LEYRAVTAAE
LPACLAVYKE TAERAGFGIH QDGYYLDIFN NLGNGSPVFA AFDGDAVVSF LWLAASDATA
FELYGGMSDE GSRLRANFSL KWLAIQEMKA RGITRYDFNG LLNDGVSQFK FGFADHENML
AGTWDKGLSP LYPVFAKALP LARKAVKKAR GLLKR
//
