ID B9DRM2_STRU0 Unreviewed; 407 AA.
AC B9DRM2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Peptidoglycan pentaglycine interpeptide biosynthesis protein {ECO:0000313|EMBL:CAR41423.1};
GN Name=murM {ECO:0000313|EMBL:CAR41423.1};
GN OrderedLocusNames=SUB0607 {ECO:0000313|EMBL:CAR41423.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR41423.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008694}.
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DR EMBL; AM946015; CAR41423.1; -; Genomic_DNA.
DR RefSeq; WP_012658130.1; NC_012004.1.
DR AlphaFoldDB; B9DRM2; -.
DR STRING; 218495.SUB0607; -.
DR KEGG; sub:SUB0607; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_2_0_9; -.
DR OrthoDB; 2173585at2; -.
DR Proteomes; UP000000449; 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; 1.20.58.90; -; 1.
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; 1.
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:UP000000449}.
SQ SEQUENCE 407 AA; 46775 MW; E6484E3C5EED7908 CRC64;
MYTYKIGISE KEHDAFVLAN PKCNLLQSSK WATIKDNWDH EIIGFYDNKT LVASTTLLIK
KLPLGKSLIY IPRGPIMDYS DFELVDFVLE SLKKYGKKQK ALFIKCDPSL FLKQFSISEI
NNEIEEIDIT LSAIEFLKKR GVEWSGRTKD IAQTIQPRLQ ANIYANQFSL QTLPKKTKQA
IRTAQNKGIE TIIGGQELLE SFAQLMKKTE ERKNIHLRGL DYYQKLMETY PEDSYITMTS
LNLAERHQLL EQQLSELLTN QSKFNEKTKE GKKKETASAI SRIQQELDFL SDKMNAGSTL
VPLAATLTLI FGKTSENLYA GMDEEFKQYQ APLLTWFETA TEAFQRGCLW QNMGGIENQL
DGGLYHFKSK LNPQIEEFAG EFNIPVSLLY RPAMLAYNLR KQLRSKH
//
