ID A0A075LMT7_9BACI Unreviewed; 504 AA.
AC A0A075LMT7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0000313|EMBL:AIF65713.1};
GN ORFNames=GZ22_03000 {ECO:0000313|EMBL:AIF65713.1};
OS Terribacillus goriensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF65713.1, ECO:0000313|Proteomes:UP000027980};
RN [1] {ECO:0000313|EMBL:AIF65713.1, ECO:0000313|Proteomes:UP000027980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP602 {ECO:0000313|EMBL:AIF65713.1,
RC ECO:0000313|Proteomes:UP000027980};
RA Wang Y., Lu P., Zhang L.;
RT "Complete genome sequence of a moderately halophilic bacterium
RT Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT Tianmu mountain in China.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, 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}.
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DR EMBL; CP008876; AIF65713.1; -; Genomic_DNA.
DR RefSeq; WP_038558505.1; NZ_CP008876.1.
DR AlphaFoldDB; A0A075LMT7; -.
DR KEGG; tap:GZ22_03000; -.
DR HOGENOM; CLU_022291_4_1_9; -.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000027980; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.1390.10; MurE/MurF, N-terminal 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; 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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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:AIF65713.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|RuleBase:RU004135};
KW Reference proteome {ECO:0000313|Proteomes:UP000027980}.
FT DOMAIN 26..97
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..317
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 339..424
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 504 AA; 55743 MW; 2F70FC7C43C17730 CRC64;
MIINLMKQNK VQFKRIYGAS STIANIVRFD SRYVTKDDVF VCIQGDNHDG HAFIEDSIAK
GAAIIVGTDE DLLKSYYRQY EDCTFLVVED TRLAMAQMAV LLSDEAWKKL VTVAVTGTNG
KTTVAAYVRS LLNQLKLQTT SIGTCGILTS KEKLDFFKST PTTPESADLH TLFKQLESEG
EKAVVMEATS IALDQKRTAA MTFDVAIHTN LSPEHLEFHQ TMDNYRRAKL KLFKQAASAV
VNIDDEGMAN DILAMYEGKL LTYSLRKNSG ADLIAGNLIT DTEGIHFELY TAEKMYTIHA
PIFGEYNVAN LLSAVGTALH LGYDMDDITE ALKTIESPEG RFELIDTYGN RKIILDYAHT
PVALDQLLTA VNAIPHKRLI VMIMGIGIRD FGKMPKMAQT VEGRADEIIV SVDHPGFHDP
KDIIQAVCKG FSEQVQNVSS AETREEAVRL ALELSSEGDI VLLTSGQING AQLVRGEAIP
HSDHAIIHDF FESHNTEKIQ TTVS
//
