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Database: UniProt
Entry: C3XGC9_9HELI
LinkDB: C3XGC9_9HELI
Original site: C3XGC9_9HELI 
ID   C3XGC9_9HELI            Unreviewed;       464 AA.
AC   C3XGC9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211};
DE            EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211};
GN   ORFNames=HRAG_01125 {ECO:0000313|EMBL:EEO24068.1};
OS   Helicobacter bilis ATCC 43879.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=613026 {ECO:0000313|EMBL:EEO24068.1, ECO:0000313|Proteomes:UP000005085};
RN   [1] {ECO:0000313|EMBL:EEO24068.1, ECO:0000313|Proteomes:UP000005085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43879 {ECO:0000313|EMBL:EEO24068.1,
RC   ECO:0000313|Proteomes:UP000005085};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:EEO24068.1}.
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DR   EMBL; ACDN02000031; EEO24068.1; -; Genomic_DNA.
DR   RefSeq; WP_005218497.1; NZ_KI392038.1.
DR   AlphaFoldDB; C3XGC9; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_2_2_7; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000005085; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
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-UniPathway.
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   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEO24068.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005085}.
FT   DOMAIN          8..105
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          305..403
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   464 AA;  52052 MW;  8AD64F8465873463 CRC64;
     MDFYQLRVHF IGIGGIGVSG LARFLKAQGA IVSGSDIKDT SITQTLRDEG IAINIPHNKE
     VIANKDLIIH SAIIKDSNIE IIESKRLNKE ILSRKEALKI LLSKKRVLSI CAAHGKSSTS
     AILAAILPHS GAIIGAISKE FNSNVRVSKD DLLVFEADES DKSFLNSNPY KSIVINAEAE
     HLESYDNDFK KLQDAYLSFM QQGKHVVLNM QCEILQNLYV RLKDSGFKSS AIICLYPDID
     IQNITYELKD LLPYTTFTLK DLGRFSIYGI GYHNALNASI AVLSAMDLLP LEEIKRNLLA
     FKGIKKRFDI LQNLSDNTPC IIDDYAHHPT EIVATLEATR KYAKLLEAQK VLKKDSKNSY
     KITAIFQPHK YSRLRDNLEA FCKCFRDCDR LVILPVWAAG EEPINFDFAT LFSEYKPIFA
     SKIKRDKEKI LLLDSKNCVI ETLSEGIIIG LGAGDITYQL RGEQ
//
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