ID A5UJE5_METS3 Unreviewed; 426 AA.
AC A5UJE5;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Cell wall biosynthesis protein, MurD-like peptide ligase family {ECO:0000313|EMBL:ABQ86323.1};
GN OrderedLocusNames=Msm_0118 {ECO:0000313|EMBL:ABQ86323.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86323.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86323.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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DR EMBL; CP000678; ABQ86323.1; -; Genomic_DNA.
DR RefSeq; WP_011953694.1; NZ_CP117965.1.
DR AlphaFoldDB; A5UJE5; -.
DR STRING; 420247.Msm_0118; -.
DR EnsemblBacteria; ABQ86323; ABQ86323; Msm_0118.
DR GeneID; 78816743; -.
DR KEGG; msi:Msm_0118; -.
DR PATRIC; fig|420247.28.peg.122; -.
DR eggNOG; arCOG02818; Archaea.
DR HOGENOM; CLU_629483_0_0_2; -.
DR BioCyc; MSMI420247:GHWZ-119-MONOMER; -.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABQ86323.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 118..240
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 426 AA; 46551 MW; 4AECE56CD9696F06 CRC64;
MKAAVIGLGV EGKKAVNSLL SHGWEVYATD LNSNVDLSDL ELPMISMNLV SGGETVSIVS
DNLTVDLGFS NSSAIEECDA IAISPSMYGG AFADKLLEKG KLLSNVVTKH KDIFTIGITG
TNGKTTSVHM LKSILENAGK KVLVGGNGGG GFSGYYDLIL EASNDDYDIL LVEVCDMTLD
FCNYCFDFDM VGLTNIGNDH MDVHKTIANY KNTLVRFFEG KTAFTAFNQD FNADFKEVAS
KAIPFFEYDE KLQVWGRFNA LNAGLVAAIA TELKIPKDII MGSLADFKAV EGRMNVYKIN
NASIFVGKTD NSDALTSVLN ENDFYALFIG TPRANEEHRL SILDEAVKYN PEVIVLFPGL
DDTVDMGLYR LNRLGYEGRI EVANSLDEII ALIAEFSHED ALFIGGNGQE AIIEIQERIR
LLSENL
//
