GenomeNet

Database: UniProt
Entry: U2TEF9_9FIRM
LinkDB: U2TEF9_9FIRM
Original site: U2TEF9_9FIRM 
ID   U2TEF9_9FIRM            Unreviewed;       467 AA.
AC   U2TEF9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000256|HAMAP-Rule:MF_00046};
GN   ORFNames=HMPREF1985_01382 {ECO:0000313|EMBL:ERL04603.1};
OS   Mitsuokella sp. oral taxon 131 str. W9106.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Mitsuokella.
OX   NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL04603.1, ECO:0000313|Proteomes:UP000016614};
RN   [1] {ECO:0000313|EMBL:ERL04603.1, ECO:0000313|Proteomes:UP000016614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W9106 {ECO:0000313|EMBL:ERL04603.1,
RC   ECO:0000313|Proteomes:UP000016614};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC         Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP-
CC         Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
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:ERL04603.1}.
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; AWVT01000011; ERL04603.1; -; Genomic_DNA.
DR   RefSeq; WP_021771641.1; NZ_KI273058.1.
DR   AlphaFoldDB; U2TEF9; -.
DR   STRING; 1321781.HMPREF1985_01382; -.
DR   PATRIC; fig|1321781.3.peg.1303; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_9; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000016614; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
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   HAMAP; MF_00046; MurC; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   NCBIfam; TIGR01082; murC; 1.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 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   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00046};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00046}; Reference proteome {ECO:0000313|Proteomes:UP000016614}.
FT   DOMAIN          14..112
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          117..296
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          318..400
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         119..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   467 AA;  50138 MW;  DC42B1CB71BF2EF4 CRC64;
     MLKHLKELNH IKKLHFVGIG GAGMSPLAKI MLELGYEVTG SDRENSSIIE NLVRLGAKVS
     LGGQKAGNVR GADAIVVSTA IPYDNPEVLA ARDLGIPKLH RSDINAALVN AYKGIAVAGA
     HGKTTTTSML GVVLSEAGVS PTVVVGGEVP DLGTNARLGT GEYLVSEADE SDGSFLKLRP
     HIAVVTNVED DHMDHYGTME NIIKAFMKFI ENVDKGTGWA VLCSDNANLR HIAERIDRKY
     ITYAIDHEAD YRATHVVTNG TGISFDVVHQ KERLGHVTLN IPGRHNVLDA LACIVTGLSI
     GVPFEKLAAG LSVFHGAKRR FETKGRVRGV WVVDDYAHHP TEIAATLKAA KETKPQRLIC
     AFQPHRYSRT QLLADEFGKA FASADLLVLT DVYAAGEAPI PGVSGHTIEA EVRRQSGQEI
     HYVEHCEDVA AELASLVQDG DLVITMGAGD IYKAGEALVR MLKGLGS
//
DBGET integrated database retrieval system