ID K6DQS3_9BACI Unreviewed; 462 AA.
AC K6DQS3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide synthase {ECO:0000313|EMBL:EKN70699.1};
GN ORFNames=BABA_04639 {ECO:0000313|EMBL:EKN70699.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70699.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN70699.1, 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:EKN70699.1}.
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DR EMBL; AJLS01000036; EKN70699.1; -; Genomic_DNA.
DR RefSeq; WP_007083961.1; NZ_AJLS01000036.1.
DR AlphaFoldDB; K6DQS3; -.
DR STRING; 1117379.BABA_04639; -.
DR PATRIC; fig|1117379.3.peg.962; -.
DR eggNOG; COG0770; Bacteria.
DR OrthoDB; 9801978at2; -.
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-KW.
DR GO; GO:0009058; P:biosynthetic process; 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 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 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT DOMAIN 111..298
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 322..400
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 462 AA; 51754 MW; 7DB41D4B142C68E2 CRC64;
MQPLLVKDIR QLLQGKLING SENWQAQDAI YYNRHEHRNR YSLMFVSRGD TINWDAINRK
GPSLVISDKP EPELKLALPN TTVIKVESLV QAYWKFIEYY RGLFDIPVVT ITGTCGKTTT
KDMIKHILSE NRNVQASESS KNEPRRSFPY LMGIDEKTDA AVFEHGLGNS GNIKHQCMIY
QPTIGIITNI GVHHLDGCKN LEGYIRAKSE IVEGIRKDGT LILNADDENT RKVSLKLFKG
KVIYVGVNMQ SDFRASDIKF ANNGMEFTLH FNDKTYEAFI SGYGEHQVYN ALAALAAVHE
MGMDIEEAIT RLGSYKNMTR HLEFFTGVGG STIIDDTWTI NPTSIEAALK VLDSIGSGKN
VILVLGDINR LGNFEKKYHR EIGTLVAKRN IHTLITIGNK AEEIARQASQ DGSKANIHMF
KDVKGLKEVL DPILDSNAIL LIKGPMSSRS MIDFANSLKK DS
//
