ID A0A182C7D2_9BACT Unreviewed; 449 AA.
AC A0A182C7D2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AT15_07925 {ECO:0000313|EMBL:OAA31414.1};
OS Kosmotoga arenicorallina S304.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=1453497 {ECO:0000313|EMBL:OAA31414.1, ECO:0000313|Proteomes:UP000077339};
RN [1] {ECO:0000313|EMBL:OAA31414.1, ECO:0000313|Proteomes:UP000077339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S304 {ECO:0000313|EMBL:OAA31414.1,
RC ECO:0000313|Proteomes:UP000077339};
RA Pollo S.M., Charchuk R., Nesbo C.L.;
RT "Kosmotoga genome sequencing.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:OAA31414.1}.
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DR EMBL; JFHK01000004; OAA31414.1; -; Genomic_DNA.
DR RefSeq; WP_068346539.1; NZ_JFHK01000004.1.
DR AlphaFoldDB; A0A182C7D2; -.
DR STRING; 1453497.AT15_07925; -.
DR PATRIC; fig|1453497.3.peg.1575; -.
DR OrthoDB; 9804126at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000077339; 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; 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 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:OAA31414.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000077339}.
FT DOMAIN 2..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 105..280
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 310..383
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 449 AA; 50604 MW; 9C5E13B1A45A0CE7 CRC64;
MKYHFIGIGG IGMSGLALHL AAEGHVICGS NFEENERVEY LRGKNIQIMI GHSPHNISSP
DIVVRTTAIS GNNPELVAAV KNGIPVLYRM ELLKRVLSEK QSICVTGTDG KTTTTAMLSK
IFIDAGKDPT VFLGGKVPFL EHENYRRGSS IAITELDESD GFFASFKVNH ALFTNVRFDH
LEHYGNNHEH FLDHLILFSK GVSGKIVYNR DDDMLRMLFE GKESVSFGKY DSDYRFERLS
IKGLRQTFEV FEAENSLGVF ELNLPGEYNI YNALGAIAMA RQFDISPEII RNSLASFVSA
DRRFTVRGYN EEKDLYLIDD YAHTPDEIRN TIKGAREAFP DRKLAIVFQP HRYSRLAREN
GRFAASLKGA DEVCVFKLYD AYEKGSSALS ETEVLDGLRK HNVPSHHYVD YHQVLEWVEE
QKKAVILFLG AGDITELSRL SAFKVNSAR
//
