ID A0A1F5B0E5_9BACT Unreviewed; 447 AA.
AC A0A1F5B0E5;
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=A2Z10_03615 {ECO:0000313|EMBL:OGD24099.1};
OS Candidatus Azambacteria bacterium RBG_16_47_10.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1797292 {ECO:0000313|EMBL:OGD24099.1, ECO:0000313|Proteomes:UP000176639};
RN [1] {ECO:0000313|EMBL:OGD24099.1, ECO:0000313|Proteomes:UP000176639}
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:OGD24099.1}.
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DR EMBL; MEYI01000014; OGD24099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5B0E5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000176639; 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 43..260
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 281..364
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 447 AA; 49555 MW; D1E4444DC1CA49B9 CRC64;
MAIKKIIRTI TPESFISAYH CSLAFLAALW YRFPSESMVV IGITGTKGKS STIFMLAKIL
EGAGLKVGVS SSIMFKINEN EWLNPYHMTM AGRFRLQQFL YQAKTAGCTH VLIETTSEGI
KQHRHRFINF DVAVFTNLSP EHIEAHGGFE NYKRAKGKLF EALSRTKQKT LNGKKIEKIA
VVNTDNEHAA YFMEFHADKT YGFGIRGMCA LPAEGRHVCA EASGVVASAD GVSFTLEKVP
FRLRVLGEFN AVNAVCASVT AYSIGIPYAA ARTALEKIEE IPGRMKFIKE GQKFIAIIDF
AHTPGSFEQV FAAVRTLKDP KGRIIAVFGS AGGGRDVWKR PELGAIAAKN ADIIFLTADD
PYQESVEAIC DDIKKGITAL PFRGKLEVIP DRRMAIKAAM EAARWNDIVL FIGKGTEQTI
AIGDEKLPWN EEEIVIQELR NMLYDRT
//
