ID A0A1J5FD29_9BACT Unreviewed; 438 AA.
AC A0A1J5FD29;
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=AUK10_00960 {ECO:0000313|EMBL:OIP54375.1};
OS Candidatus Gracilibacteria bacterium CG2_30_37_12.
OC Bacteria; Candidatus Gracilibacteria.
OX NCBI_TaxID=1805211 {ECO:0000313|EMBL:OIP54375.1, ECO:0000313|Proteomes:UP000182482};
RN [1] {ECO:0000313|EMBL:OIP54375.1, ECO:0000313|Proteomes:UP000182482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_37_12 {ECO:0000313|EMBL:OIP54375.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIP54375.1}.
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DR EMBL; MNYO01000032; OIP54375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FD29; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000182482; 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; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 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 42..251
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 272..354
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 438 AA; 49036 MW; 41F39E609F9D207B CRC64;
MNFLRSLISL DSPIRIFYHY LRGVLAFHLY GNPARDMIVI GITGSKGKTT VTNLIAKGLE
HAGKKVFMFS TANYSINGQW SDNNIKMTSP SPFVLQRLLK QAKAAGCEYV VIETSSHSIF
YNRNYGIDYD VAVLTNISQD HLDLHHTMDN YAKTKLELFK NLVTYRRKPG VKKIAVVNID
SDYASMFLSE TTPDIMYTYG LTPNAQVRSQ NIHYLKEGTE FEIKMPSNTL SITTKLRGSF
NVSNILAAVS VLISQKIDVA TIVNAIESVK VIPGRLEEIE NVRGITVFVD YAHTEDSLRN
VLETMKQMDG IGRIITVFGA TGDRDTSKRP KMGRIVDSLS DVVILTEDDN YTENSLKIIK
EVSMGIKRKE GEGFWIIPSR MDAIRTALVI AEKGDVVLIA GKGAESSQIT NTGPIAWDDR
IVTRKILQEI SENEMMMR
//
