ID A0A0G0CJW7_9BACT Unreviewed; 426 AA.
AC A0A0G0CJW7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE SubName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000313|EMBL:KKP43722.1};
GN ORFNames=UR31_C0001G0046 {ECO:0000313|EMBL:KKP43722.1};
OS Parcubacteria group bacterium GW2011_GWA2_33_14.
OC Bacteria.
OX NCBI_TaxID=1618807 {ECO:0000313|EMBL:KKP43722.1, ECO:0000313|Proteomes:UP000034294};
RN [1] {ECO:0000313|EMBL:KKP43722.1, ECO:0000313|Proteomes:UP000034294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP43722.1}.
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DR EMBL; LBOS01000001; KKP43722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0CJW7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000034294; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..249
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 271..350
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 426 AA; 48432 MW; E52C2A376F6F9EEE CRC64;
MNIKKSIKNL APAFLLNFYH YGLALIGTVV FWFPGNKLIV IGVTGTSGKS TTVDFITKIL
EENGNSVASL SSIRFKIKAK EWKNELKMTM PGRFMIHKFL REAVNEKCQY AVLEVTSEGI
KQYRHKFINF NTVVFTNLSP EHIESHGGFE NYRNEKFKLF KATKNIHIIN IADDNAQYFW
DISAKEKIGF KLKTQNSKLK NTTQDSKIIE ADNVEIIKDG LLFKIQDTRF NISLMGEFNI
YNTLAAISVG LSQGISLEIC KKALEKVRGI FGRMEIVSKN PLIIVDYAHT PEQLEQVYKS
LPGKNLVCVF GSCGGGRDKW KRPVLGKIAE QYCKEIIITN EDPYDEDPLE IMEQIASGIN
NRDYHIVLDR KEAIKKALGL SKDENTVIIT GKGSEVWMCV DGGRKIPWSD KEIIKEEILL
KNKKYV
//
