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Database: UniProt
Entry: A0A0U5AZ90_9BACT
LinkDB: A0A0U5AZ90_9BACT
Original site: A0A0U5AZ90_9BACT 
ID   A0A0U5AZ90_9BACT        Unreviewed;       474 AA.
AC   A0A0U5AZ90;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=UDP-N-acetylmuramate {ECO:0000313|EMBL:BAU23049.1};
GN   ORFNames=THC_0657 {ECO:0000313|EMBL:BAU23049.1};
OS   Caldimicrobium thiodismutans.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX   NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23049.1, ECO:0000313|Proteomes:UP000068196};
RN   [1] {ECO:0000313|EMBL:BAU23049.1, ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|EMBL:BAU23049.1,
RC   ECO:0000313|Proteomes:UP000068196};
RX   PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring, and emended description of the genus
RT   Caldimicrobium.";
RL   Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN   [2] {ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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DR   EMBL; AP014945; BAU23049.1; -; Genomic_DNA.
DR   RefSeq; WP_068513262.1; NZ_AP014945.1.
DR   AlphaFoldDB; A0A0U5AZ90; -.
DR   STRING; 1653476.THC_0657; -.
DR   KEGG; cthi:THC_0657; -.
DR   PATRIC; fig|1653476.3.peg.677; -.
DR   OrthoDB; 9804126at2; -.
DR   Proteomes; UP000068196; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   CDD; cd00636; TroA-like; 1.
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   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:UP000068196}.
FT   DOMAIN          3..100
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          109..299
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          320..387
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   474 AA;  52673 MW;  34DDDDAC5C1099A2 CRC64;
     MRVYFIGIGG IGMSGVAGLC RGLGFEVCGS EENPLYPPSS FLLKELGIEV FKPSEENLLK
     FKPDLVVVGN AISSSHIEVA KAKALRIPLL SFPEFIENFI LDRKKALVIA GTHGKTTTSA
     LLSFTLLKLE KSPTFLVGGI LKDTGKNFAY GKGEFMLLEG DEYPSAFFNK NPKFLHYKPF
     GLILTSLEYD HADVYPDINA LKEAFKKLLK LLPMEGILVF NQDDPNLVEI VEASQPLCKI
     ITYGKGKADF KLVGSEVSLG GGGFRSKGLA KAKDGEVFEI DLSIPGDYNL LNALSTIALL
     ETLGFHRKDI LEAIKDFKGV QRRQEILFAS ETLLVIDDFA HHPTALALTL KELKKAFQPE
     KTILFFEPRT NSSKRKVFQR DYVEALNEAD LIGIKVPPGL ERIPFQDRID LEQLRNDLED
     LGKRAFILEK GLIPPEFFDL TQKSLVVFMS SAFMQEEIKL FFKGIGKSHA QNTG
//
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