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Database: UniProt
Entry: W4M725_9BACT
LinkDB: W4M725_9BACT
Original site: W4M725_9BACT 
ID   W4M725_9BACT            Unreviewed;       472 AA.
AC   W4M725;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ETSY2_22985 {ECO:0000313|EMBL:ETX05427.1};
OS   Candidatus Entotheonella gemina.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC   Entotheonella.
OX   NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX05427.1, ECO:0000313|Proteomes:UP000019140};
RN   [1] {ECO:0000313|EMBL:ETX05427.1, ECO:0000313|Proteomes:UP000019140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX   PubMed=24476823; DOI=10.1038/nature12959;
RA   Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA   Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA   Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA   Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT   "An environmental bacterial taxon with a large and distinct metabolic
RT   repertoire.";
RL   Nature 506:58-62(2014).
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:ETX05427.1}.
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DR   EMBL; AZHX01000952; ETX05427.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4M725; -.
DR   PATRIC; fig|1429439.4.peg.3917; -.
DR   HOGENOM; CLU_028104_0_2_7; -.
DR   Proteomes; UP000019140; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-KW.
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; IPR005757; Mpl.
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   NCBIfam; TIGR01081; mpl; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019140}.
FT   DOMAIN          8..105
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          114..302
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          322..403
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   472 AA;  51928 MW;  3A4531B67D6A88E0 CRC64;
     MIPEAPHHIH LVACCGTAMG SLAGMLKARG YHVTGSDQHV YPPMSTQLEA WGIPIYEGFD
     PAHLDPRPDL VVVGNVVTRD NAEAAATREL GIPAMSFPQA LAHFFIQNRQ GVVVTGTHGK
     STTTALIAWV LAHAECDPNV FVGAVMRNFD STFRLGDGPH MVIEGDEYDS AYFDKGPKFL
     HYRPRTAVLT SMEFDHADIY RDFEHVRSAF VRFLGIMPAE GYLVACADHY QVREVIANNP
     VASAVQTYGI EPGADWRAET YTSSPEGTEL TVSYQNQPYG QFRAPLYGPH NIQNVLATIA
     VAHHLGLTPA QIASGLATYA HIKRRLEVRG TVGEVTVIDD FAHHPTAVQV TLEGVRQAYP
     GQRIWAVFEP RTATSRRNVF QQDYIQALQG ADYVILSDIH RKESLAPSER LSPEAIVEAL
     RHHIVGADFY AGTSGIIDQL CRDTRPGDVV IVMSNGGFDN IHERLLTALA ER
//
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