GenomeNet

Database: UniProt
Entry: W6TDU8_HOLOB
LinkDB: W6TDU8_HOLOB
Original site: W6TDU8_HOLOB 
ID   W6TDU8_HOLOB            Unreviewed;       536 AA.
AC   W6TDU8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0000313|EMBL:ETZ06971.1};
GN   ORFNames=P618_200869 {ECO:0000313|EMBL:ETZ06971.1};
OS   Holospora obtusa F1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC   Holospora.
OX   NCBI_TaxID=1399147 {ECO:0000313|EMBL:ETZ06971.1, ECO:0000313|Proteomes:UP000019112};
RN   [1] {ECO:0000313|EMBL:ETZ06971.1, ECO:0000313|Proteomes:UP000019112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ETZ06971.1,
RC   ECO:0000313|Proteomes:UP000019112};
RX   PubMed=25115770;
RA   Dohra H., Tanaka K., Suzuki T., Fujishima M., Suzuki H.;
RT   "Draft genome sequences of three Holospora species (Holospora obtusa,
RT   Holospora undulata, and Holospora elegans), endonuclear symbiotic bacteria
RT   of the ciliate Paramecium caudatum.";
RL   FEMS Microbiol. Lett. 359:16-18(2014).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|RuleBase:RU004135}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|ARBA:ARBA00005898}.
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:ETZ06971.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWTR02000074; ETZ06971.1; -; Genomic_DNA.
DR   RefSeq; WP_021827047.1; NZ_AWTR02000074.1.
DR   AlphaFoldDB; W6TDU8; -.
DR   STRING; 1399147.P618_200869; -.
DR   eggNOG; COG0769; Bacteria.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000019112; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-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   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; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   NCBIfam; TIGR01085; murE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 2.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU004135};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   ECO:0000256|RuleBase:RU004135};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|RuleBase:RU004135};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|RuleBase:RU004135}; Ligase {ECO:0000313|EMBL:ETZ06971.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW   ECO:0000256|RuleBase:RU004135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019112}.
FT   DOMAIN          111..274
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          376..462
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   536 AA;  59952 MW;  98265F64C2D1CCDE CRC64;
     MITLQDVCCA LGVNLGIIQE NFSDVSLHSE RSGPDVLFWA SPSAQYTVED LAYMAWEKGV
     RVILAWGSNY RCFQNPNCLN QVCIFQNFPK NTVEILANVF YPGRPSSKCA VTGTNGKTST
     VSFLSQLWKT SKIPYVSMGT LGIQGNLNFD FSSSYINTAD YLTLSCVLHT SAKKKIQHFA
     YEASSHGLQQ LRIPADAVDI GIWTSFSQDH LDYHKTMEAY WSAKFSLGSL CKKAWLVNDT
     VYRKFMLMDS SSVSYGQNTP SDITFSDLSS SRAGGLRSLE KEFQQSFLSQ MQCDVLCYGL
     GKNTSLWAEC FIYKQSCKGA EVLIRIDSYV WRGIIPLVGS FQCENLVAAL GAFYLLGGNL
     DDAFHIIASG SIQTPSGRLE KVCDGPLGGG GIYIDYAHTP DALYQVLRTL KALKPERLGV
     VFGCGGERDK EKREKMGKIA QENAHWVIIT DDNPRYEDPE KILNDIQRGC PNAQRIRCRR
     TAIEAAISYM KQGDILLIAG KGHEAFQWVR DEKRVFQDNQ VVHERMKKLN KDSIIQ
//
DBGET integrated database retrieval system