ID A5CD83_ORITB Unreviewed; 489 AA.
AC A5CD83;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase {ECO:0000313|EMBL:CAM79765.1};
DE EC=6.3.2.13 {ECO:0000313|EMBL:CAM79765.1};
GN Name=murE {ECO:0000313|EMBL:CAM79765.1};
GN OrderedLocusNames=OTBS_0699 {ECO:0000313|EMBL:CAM79765.1};
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM79765.1, ECO:0000313|Proteomes:UP000001565};
RN [1] {ECO:0000313|EMBL:CAM79765.1, ECO:0000313|Proteomes:UP000001565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong {ECO:0000313|EMBL:CAM79765.1,
RC ECO:0000313|Proteomes:UP000001565};
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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 ---------------------------------------------------------------------------
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; AM494475; CAM79765.1; -; Genomic_DNA.
DR RefSeq; WP_011944612.1; NC_009488.1.
DR AlphaFoldDB; A5CD83; -.
DR KEGG; ots:OTBS_0699; -.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_022291_3_1_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001565; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.1390.10; MurE/MurF, N-terminal 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; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
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; PF01225; Mur_ligase; 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 SUPFAM; SSF63418; MurE/MurF N-terminal 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:CAM79765.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|RuleBase:RU004135};
KW Reference proteome {ECO:0000313|Proteomes:UP000001565}.
FT DOMAIN 15..77
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 97..309
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 330..416
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 489 AA; 54393 MW; 8B9224B5385A5260 CRC64;
MESNNIIEII KKLNIRNIAI TAQSAEPNQI FFALPGISRH GNDFIDIALA NGASLIITDQ
AHITSYSNVI VVKNITLVMK DIVNYLYPKF PKYLVAVTGT DGKTSVVNYF QQLCMLAGEQ
AASIGTLGVI TTNDHLNKRL NQNKTKPECA TTMSYIQTRY LLHQLATNGI NFVALEASSH
GLDQNRLMDI KFQAAAFTSF SRDHLDYHKT MNKYLDAKLK LFKENIVSNG IAIVNNNINE
LSIIQSKITD EFGLKLLSVE QQGDIQIINV QSSLNGQKVH FRYKNSDYKF EVLVIGRVHI
TNILIALLLA VNAGFDSAKL IPLLSNLKPI KGRMEKIQFG NCYAFVDYAL TPNALATMLT
ELRTLNSKGR LITIFGGSEN RDAIARRMQM GIVASKLSDL VIVTDQDSGN EDPAAIRKEI
LQVAPSAIEI PNRGEAIKYA ISIMVDNDIL LIAGKGHETR QVLKGRIINY NDMEQVKLHL
KQLNKMSNQ
//
