ID A0A1F5NTX9_9BACT Unreviewed; 421 AA.
AC A0A1F5NTX9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2720_04495 {ECO:0000313|EMBL:OGE80790.1};
OS Candidatus Doudnabacteria bacterium RIFCSPHIGHO2_01_FULL_46_24.
OC Bacteria; Candidatus Doudnabacteria.
OX NCBI_TaxID=1817825 {ECO:0000313|EMBL:OGE80790.1, ECO:0000313|Proteomes:UP000178892};
RN [1] {ECO:0000313|EMBL:OGE80790.1, ECO:0000313|Proteomes:UP000178892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGE80790.1}.
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DR EMBL; MFEL01000018; OGE80790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5NTX9; -.
DR STRING; 1817825.A2720_04495; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000178892; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; 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; IPR018109; Folylpolyglutamate_synth_CS.
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; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU004135};
KW Cell division {ECO:0000256|RuleBase:RU004135};
KW Cell shape {ECO:0000256|RuleBase:RU004135};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135}.
FT DOMAIN 48..248
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 268..354
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 421 AA; 46175 MW; 397B5527CA0E6967 CRC64;
MIVGVHAIKN LIKKLVGRRV VSGYHRFLSW LAAVVYGNPS EKLVVIGVTG TNGKSTTVNL
IAKILEEAGP PAGGKVVATS TVNFKIGSDE KLNDLKMTMP GRFFLQSILA RGVKVGCTHA
VLEVSSEGIE HHRHRGVHFD VCVFTNLTPE HLEAHGGFEN YKRAKLKLFA QAKKAIVANV
DDPYYAEFTN FRVPQVISFG QNSNADIRGQ RLTVAEQGIS FEVGNQSFNL HLKGRFDFYN
ALAAIATAKA LGIDLAVCRQ ALEKVQNIPG RMEIIDGPNF KVLVDYAPEP ESLRQMYASI
VQWPKNRIIH ILGSTGGGRD VSRRKILGQI ADQFADVVIV TNEDPYDDDP QQIIDDVAAG
SLKAIKILDR REAIAKALSL ARAGDLVIVT GKGAEQKMAV RGGYIQWDDR KLIREELAKI
S
//
