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Database: UniProt
Entry: A0A145Q4U5_9BACT
LinkDB: A0A145Q4U5_9BACT
Original site: A0A145Q4U5_9BACT 
ID   A0A145Q4U5_9BACT        Unreviewed;       591 AA.
AC   A0A145Q4U5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Mur ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GEMMAAP_14720 {ECO:0000313|EMBL:AMW06892.1};
OS   Gemmatimonas phototrophica.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW06892.1, ECO:0000313|Proteomes:UP000076404};
RN   [1] {ECO:0000313|EMBL:AMW06892.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW06892.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA   Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT   "Functional type 2 photosynthetic reaction centers found in the rare
RT   bacterial phylum Gemmatimonadetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN   [2] {ECO:0000313|EMBL:AMW06892.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW06892.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA   Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT   "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT   bacteria in diverse environments.";
RL   Environ. Microbiol. Rep. 8:139-149(2016).
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DR   EMBL; CP011454; AMW06892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A145Q4U5; -.
DR   STRING; 1379270.GEMMAAP_14720; -.
DR   KEGG; gph:GEMMAAP_14720; -.
DR   eggNOG; COG0769; Bacteria.
DR   Proteomes; UP000076404; 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:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic 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   PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 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   Reference proteome {ECO:0000313|Proteomes:UP000076404}.
FT   DOMAIN          187..406
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          432..494
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   591 AA;  62955 MW;  EB93E9F36526F3BA CRC64;
     MLDSRRLTGA NWWSEQPGAV LEVRNAEAID RRALEQWPRE VRVLCDALGW PSGSPNAQQH
     GVLSVCFLAA PLDGLMTATT VAEQAWVRAE LWVRSQDGDA DAAAWLLSST PTVHDALRTR
     YDNERAPLVA ACAVVAEATK RGCSWQLDED MVSVGSGVYG LSWPLDRVPV AELVTWYTVA
     DVPVVLVTGS NGKTTTTRLV TAMWRATGVT VGLSCSDGVF VHDDIGTREL AEGDYTGPGG
     ARLVLRDRAV QAAVLETARG GMLRRGLATS RAHAAVITNI SADHFGEYGV ESLGDLARVK
     ATVARILVPD ALLVLNADDE HLRALGAAME REHPNAVAWF SQDAAHPLVQ RGVQLHGYGA
     VVCDGRLMLA EQGVWSDAGA LLHMPLTLNG LAPHNVENAL AASLAASVAG VPFAAVHRAL
     HTFGADAGDN AGRLHRRVLG DVTVLVDYAH NPDGMRVLGA TAMAIPAARR LLVLGQAGNR
     DDAQLVALAQ AAWASARYDR VFLKEMPEML RGREPGDVTR VLRAALLEAG APADVISEWP
     SELDAVRAAL AWAQPGDLLV LPTHAQKEVV DALLNALEAQ GWYAGEPLAP L
//
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