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Database: UniProt
Entry: A0A087AR35_9BIFI
LinkDB: A0A087AR35_9BIFI
Original site: A0A087AR35_9BIFI 
ID   A0A087AR35_9BIFI        Unreviewed;       525 AA.
AC   A0A087AR35;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diami nopimelate ligase {ECO:0000313|EMBL:KFI61235.1};
DE            EC=6.3.2.7 {ECO:0000313|EMBL:KFI61235.1};
GN   ORFNames=BIGA_0668 {ECO:0000313|EMBL:KFI61235.1};
OS   Bifidobacterium pullorum subsp. gallinarum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61235.1, ECO:0000313|Proteomes:UP000029046};
RN   [1] {ECO:0000313|EMBL:KFI61235.1, ECO:0000313|Proteomes:UP000029046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61235.1,
RC   ECO:0000313|Proteomes:UP000029046};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI61235.1}.
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DR   EMBL; JGYX01000002; KFI61235.1; -; Genomic_DNA.
DR   RefSeq; WP_033507922.1; NZ_JGYX01000002.1.
DR   AlphaFoldDB; A0A087AR35; -.
DR   eggNOG; COG0769; Bacteria.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029046; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine 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; 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; 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|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   Ligase {ECO:0000313|EMBL:KFI61235.1};
KW   Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029046}.
FT   DOMAIN          124..342
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          362..450
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   525 AA;  57271 MW;  B59639F929BEF68B CRC64;
     MSAFTIATAA QLLERHHLLR EIIHTGGWTL DASDVPGADN PIAAVTYDTR TVTPGSMLFV
     KGRFRPEFLD GIDERGLAVY VAENDHSDRT AATGLIVDDV HKAMSLLSAE FYGRPQDELT
     VIGITGTKGK TTTAYLVHAI LNDYSNQRAA LFSSEQTCLD GRTYTDSKLT TPESLDAFRM
     MRQAADNGMR YLVMEVSSQA YKVHRVHGLT FDIGAFLNIS PDHISPIEHP TFEDYLHCKR
     QLITNSKTLV LDAACDHHRL LMQDAAMADV PVAQYAFLDG TDDTTGADSR SGIRNLFVAA
     RPDPHNRMGF LLTADGAELG PFELAMPGTF NIANAAAAVA MALKAGVPAT DPAIHAIERV
     SVPGRMERIT AGGNLVVYVD FAHNYLSCKA LVDEALRAYG NRNPRITLVA GSTGGKAIDR
     REGIVKGADG RAEAFYFTLD DPNFEDPTAI AEEMRSYVTD PRAETHVIVP REDAIRAAIE
     DARRHADRFN VVLLAGKGHE RRNIINGKPV PYEGDGPIAR RLLGL
//
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