ID K6EB87_9BACI Unreviewed; 721 AA.
AC K6EB87;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:EKN70691.1};
GN ORFNames=BABA_04599 {ECO:0000313|EMBL:EKN70691.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70691.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN70691.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN70691.1}.
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DR EMBL; AJLS01000036; EKN70691.1; -; Genomic_DNA.
DR AlphaFoldDB; K6EB87; -.
DR STRING; 1117379.BABA_04599; -.
DR PATRIC; fig|1117379.3.peg.955; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG0770; Bacteria.
DR OrthoDB; 7869153at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_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; IPR026838; YheC/D.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF14398; ATPgrasp_YheCD; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EKN70691.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT DOMAIN 110..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 721 AA; 81685 MW; 55C174E47E305E7D CRC64;
MTLIGMLHHR KDPKTVIKSY AYAAVAKAEG AKFFYFSPGS VNFVNNTIRG QVYENGKWME
RIMPFPDVIY NAGSPEKLAN SKEIIQRLKE KIPFTTHSIG NKWNINERLK EAKEFANYLI
PTEIVINTEH FFKFVTAFEK VVFKPIDGRK GKGIFFISVS ENGFLVKKDS DSIFYSKQQL
NDLIGSKLST GTYIVQPYIQ STTKSGQVFD FRLHVQKDGE GKWVITTIYP RVAPMGSIIA
NINNGGFTNY LEPFLQQEFK EEAFNIKRTL EHFSLSLANH LDELQMIHYG EVIDEIGVDV
GLDENSKIWI YEVNWRPGCP PAFYLELDVV INTIKYAMFL AKNQNTITKT IKALKQKKME
EKKEIPIIAI TGSAGKTTTK AFVASILAKK WNIFESKDYW NTTEHTKKHA AEINPAHEAI
VLEYGMAYPG VITEHCSIIQ PNISIVTNIG LAHVGNFDGD ITKVAHAKSE LIHGMDQNGV
LFLNKDDPNS TFLETQNFKG KIITIGVNSS ADYRAYDVKY NDTGMNFKMK LQGQEISLFI
PILGEHHVYN ALNAIAVADY LGFTPMEIKL GLLFRKPPRR LTIYNCRDNI TLIDDTVHSH
PQGVRAAIDV LSNIGKHRKI AIIGQMRELG GLREEEYRKV GEYVFDKEID VLITYGFRTE
EMGAQAKAKG FPAKNVYHFT NKDELNALLV KIIKKDDTIL VKGASKTNMF DIVKFLDQTF
S
//
