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Database: UniProt
Entry: A0A0G0PIN0_9BACT
LinkDB: A0A0G0PIN0_9BACT
Original site: A0A0G0PIN0_9BACT 
ID   A0A0G0PIN0_9BACT        Unreviewed;       472 AA.
AC   A0A0G0PIN0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 37.
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=UT61_C0059G0005 {ECO:0000313|EMBL:KKR28024.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWA1_39_8.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618552 {ECO:0000313|EMBL:KKR28024.1, ECO:0000313|Proteomes:UP000034793};
RN   [1] {ECO:0000313|EMBL:KKR28024.1, ECO:0000313|Proteomes:UP000034793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KKR28024.1}.
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DR   EMBL; LBXL01000059; KKR28024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0PIN0; -.
DR   PATRIC; fig|1618552.3.peg.1126; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000034793; 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:KKR28024.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          8..108
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          118..304
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          326..407
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   472 AA;  52139 MW;  2CF2F4192EA10118 CRC64;
     MNLKTIKHVH FTGIKGVGMT ALALYFRDMG KTITGSDIEE IFVTDQVLKA NDINLKIGFG
     EHNLDSKPDL VICTAAHNGL NNPEVVAAKR FHIPVMTYAE GLALVSREKK LIATCGVGGK
     TTTASMIATM LEMSAQDPSY VIGVANINPI GDAGHYDSRG KYIVAEGDDY AISPGVNNNP
     KFSLLSPKIL VVHNIAHDHP DIYKTFSDIK KTFKVFFDKF GRDDVLIASI DNEAVRKLIK
     GLKAQVITFG VDKVADYQIK NIRFQSGKTM FAVFDTKQNV FTVDLTMEVP GAYNIHNATA
     AYLVGKFLGL ADNKLKHGIE SYKGCKRRFE KIGEYRGATV YDDYAHHPNE IVEVLEATRA
     WFPKDRIVAI FQPHTFSRTK ALFSDFAKSF KGADIVGLMD IYASSREASG VGVSSKLLVK
     AIKNFNSKTY YLGDHKATLS WLKKNVKKGD ILLTIGAGDI FRLHKELIPE ST
//
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