ID J0D5M6_9BIFI Unreviewed; 538 AA.
AC J0D5M6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000313|EMBL:EJD65285.1};
GN ORFNames=HMPREF9156_00049 {ECO:0000313|EMBL:EJD65285.1};
OS Scardovia wiggsiae F0424.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Scardovia.
OX NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD65285.1, ECO:0000313|Proteomes:UP000006415};
RN [1] {ECO:0000313|EMBL:EJD65285.1, ECO:0000313|Proteomes:UP000006415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0424 {ECO:0000313|EMBL:EJD65285.1,
RC ECO:0000313|Proteomes:UP000006415};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C.,
RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Scardovia wiggsiae F0424.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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:EJD65285.1}.
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DR EMBL; AGZS01000001; EJD65285.1; -; Genomic_DNA.
DR RefSeq; WP_007147117.1; NZ_JH719939.1.
DR AlphaFoldDB; J0D5M6; -.
DR STRING; 857290.HMPREF9156_00049; -.
DR GeneID; 84814986; -.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_022291_4_2_11; -.
DR OrthoDB; 9800958at2; -.
DR Proteomes; UP000006415; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR035911; MurE/MurF_N.
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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006415}.
FT DOMAIN 143..350
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 376..455
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 538 AA; 58303 MW; 62056F568DEF8EEB CRC64;
MTTAAGSSPD TFSPTPSSHT LSLAQAIGIL DSHGQLREII ADGQWARSAD ALGTKYRDMV
FTDISYDSRD VGSQTLLFCK GRFEASYLTD ANSSGLPCYV AQEDFSGSTG AAGIIVNDVK
KSMALLSAAF FGYPSRRLTV IGITGTKGKT TTAYFTHSIL NAYSQGKAAL LSSVDNCTDG
HTFAESDLTT PESLDLFRLM CEAADNGMEY LVMEVSSQAY KVDRVYGLHF DAGAFLNISP
DHISPIEHPT FEDYFYCKRQ ITANSSHIVI NADLDHAGLV EEDALRCSTQ LSRFRLCRPP
VSANSKDVYA YPSSDGQSFL INAGTTPLGS FILSIAGDFN YANAAAAVAI VQASGMDLSS
PPVQNALHAM EKVTIAGRME TFTSPDGTVG IVDYAHNGVS TAALLDYVDK TYGSLSPRII
LITGSAGNKA YDRRREIVEA AQDRIFRFIF TTEDTDTEKV QDICEEMERY ITNTDVEHSI
IIDREEALRA AVSDAHKASG QTTVILAIGK GNERWIKQFN KHVPYEGDDA VMKGLLHG
//