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Database: UniProt
Entry: B1V4M9_CLOPF
LinkDB: B1V4M9_CLOPF
Original site: B1V4M9_CLOPF 
ID   B1V4M9_CLOPF            Unreviewed;       560 AA.
AC   B1V4M9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Mur ligase family protein {ECO:0000313|EMBL:EDT71227.1};
GN   ORFNames=CJD_3074 {ECO:0000313|EMBL:EDT71227.1};
OS   Clostridium perfringens D str. JGS1721.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT71227.1, ECO:0000313|Proteomes:UP000003188};
RN   [1] {ECO:0000313|EMBL:EDT71227.1, ECO:0000313|Proteomes:UP000003188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA   Paulsen I., Sebastian Y.;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:EDT71227.1}.
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DR   EMBL; ABOO01000026; EDT71227.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1V4M9; -.
DR   Proteomes; UP000003188; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:EDT71227.1}.
FT   DOMAIN          168..375
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          402..483
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   560 AA;  63793 MW;  C5AED1EB14ED0A53 CRC64;
     MVGRVSDLKL KDLRVLEGRN IKGEENLIFI DIEESERKRL YWLISDYEFI CRKMNMEGTL
     KEAIYNEFGG CAWLTYSNKE LALFIIESLI EGVSADKLLN EAVAKKQRIW EYNLLEECSK
     KKIDFFKEDD EIIVGYGVNS KRISKEDYEN KNYNLDLINN GVIPIVSITG TNGKTSTSRL
     IYKGFENLGY FSGLAMTGGI IINNEFVKKG DTTGFYSAKK VLTNPQVEVG VLETARGGIL
     RKGLGFKNSK VAIITSLAED HIGVDGIKDI NDLLDIKLIT TREVLPEGKV IIKAEPKLYE
     VLQTKENLVL FNSKKNEYIE KHMKNGKEAW FVEDENVIFF DGKDKNIISN IKDFKFTHDG
     NSKTNINNIL VSIAAIYEVH KNLKEVVDSL KNIECDVYNN IGRQNIIELE NFKIILDYGH
     NPEAFEELFY LANNIKRNKI ISIVSSPGDR LDEYIKELGR IAGENSDTII IKETFDRRGR
     EKLEITNLIK SGIKEVENKS VEVLSIIDEE EAIKKAISMA EEGDIIVDFT QHLDVVIPVI
     NKYLSNHGKE IIEVDLEDFH
//
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