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Database: UniProt
Entry: F9ZZP8_METMM
LinkDB: F9ZZP8_METMM
Original site: F9ZZP8_METMM 
ID   F9ZZP8_METMM            Unreviewed;       482 AA.
AC   F9ZZP8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=Metme_0258 {ECO:0000313|EMBL:AEF98707.1};
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087 {ECO:0000313|EMBL:AEF98707.1, ECO:0000313|Proteomes:UP000008888};
RN   [1] {ECO:0000313|EMBL:AEF98707.1, ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|EMBL:AEF98707.1,
RC   ECO:0000313|Proteomes:UP000008888};
RX   PubMed=22123758; DOI=10.1128/JB.06267-11;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA   Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA   Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L., Murrell J.C.;
RT   "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT   methanica MC09.";
RL   J. Bacteriol. 193:7001-7002(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MC09;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA   Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA   Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L.Y., Murrell C.;
RT   "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT   methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) 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|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
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DR   EMBL; CP002738; AEF98707.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9ZZP8; -.
DR   STRING; 857087.Metme_0258; -.
DR   KEGG; mmt:Metme_0258; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_6; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008888; Chromosome.
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:UP000008888}.
FT   DOMAIN          17..114
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          120..300
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          323..409
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   482 AA;  52019 MW;  F76EB394D20E2E3E CRC64;
     MNRPNIHPAQ ALGSIDKIHF VGIGGTGMSG IAEVLSNLGY SVSGSDIKAS PVTERLQGMG
     VKVYFEHTAA NVADVDVVVT STAVDRKNPE ITTAYANRIP VIPRAEMLAE LMRFRFGIAV
     AGTHGKTTTT SLTTMMLAEG GLDPTFVIGG RLNSAGSNAK LGLGKYLVAE ADESDASFLY
     LQPMMAVVTN IDQDHMETYG GSYNRLKDTF IKFLHQLPFY GLAVLCVDDP GVQEILPLIS
     KPVKTYGVTE TADVRAVDIK QDGLQTHFGV LRWDGLPPMQ VTLNLPGWHN MLNALAAITI
     ATSLGVEDAA IIKSLAEFNG VGRRFQINGD LEIDGGKLTL VDDYGHHPRE LAATLEALRQ
     AWPERRKVVV FQPHRYTRTR DLFEDFVEVL SSVDVLILLD VYSAGEAPIN GADGKALSRS
     IRVRGQVDPV FVQNRDDLST ILAGIVQADD VILTMGAGNV GQIAAELPQK LQEALASLRI
     SA
//
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