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Database: UniProt
Entry: A0A1Y3WFQ6_9FIRM
LinkDB: A0A1Y3WFQ6_9FIRM
Original site: A0A1Y3WFQ6_9FIRM 
ID   A0A1Y3WFQ6_9FIRM        Unreviewed;       507 AA.
AC   A0A1Y3WFQ6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000313|EMBL:OUN68650.1};
GN   ORFNames=B5G11_11875 {ECO:0000313|EMBL:OUN68650.1};
OS   Drancourtella sp. An57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN68650.1, ECO:0000313|Proteomes:UP000196207};
RN   [1] {ECO:0000313|Proteomes:UP000196207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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}.
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:OUN68650.1}.
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DR   EMBL; NFHY01000014; OUN68650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3WFQ6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000196207; 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:UniProtKB-KW.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196207}.
FT   DOMAIN          118..325
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          345..424
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   507 AA;  56958 MW;  189E7FC6E8AC1A19 CRC64;
     MSQRKSDTLK TYADLMEECG LLVKAEFFGQ EDTHPEVLTY DSREVTENTM FICKGAAFKE
     EYLTSAVEKG AILYISEKEY DTGKDIPHIL VKDIRKAMAV LADVFYGSAW KELTVTGIGG
     TKGKSTSAYY MKSVVDDYMK ETGKPESAVI SSIDIYDGVS RVESHITTPE AVELQRHFRN
     AVDSGITFAE MEVSSQALKY NRVDRMRFDV GIFLNISEDH ISPIEHPDFE DYFTSKMKMF
     AQTDHAVVNL DADFSDRILE AARAAGDLTT FSQKDEGADY FAYNIRKDGH ETKFSVRSKD
     GEEDYVLTMP GLFNVENAVA VIAAAKILGI PDSCIHSGLE KARSSGRMEL YASRDKKIIA
     IVDYAHNKLS FEKLFSSTKE EYPDYAIKSV FGCPGKKAYI RRKDLGTIAG QYSEKVYLAA
     EDPGYEPVEE ISGDIAQYVK AQNCPYVMIE DRGEAIRTAI EESEDKTVIL VTGKGNETRQ
     KYGSEYIDCP SDVEYVKKYL EIYDQTH
//
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