ID B3EPD1_CHLPB Unreviewed; 476 AA.
AC B3EPD1;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:ACE03809.1};
GN OrderedLocusNames=Cphamn1_0858 {ECO:0000313|EMBL:ACE03809.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03809.1};
RN [1] {ECO:0000313|EMBL:ACE03809.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE03809.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001101; ACE03809.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EPD1; -.
DR STRING; 331678.Cphamn1_0858; -.
DR KEGG; cpb:Cphamn1_0858; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_0_2_10; -.
DR OrthoDB; 9804126at2; -.
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-KW.
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; 3.40.50.720; NAD(P)-binding Rossmann-like 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; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACE03809.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 4..97
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 110..299
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 320..400
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 476 AA; 52217 MW; 8E15415A29800D2C CRC64;
MSSLYFIGIA GTAMASVAVA LSRAGHRVAG SDSALYPPMS DYLNKHRIPC HTGFDPLNIL
RDAPDVIVVG NAISRGNPEL EAALNEHMNL VSMPEIVRRE LIGKNRSIVI TGTHGKTTTT
SLTAWLFEHA GLTPGFLIGG IAENFNAGCR ASGKKKGGHF ITEGDEYDTA YFDKRSKFLH
YRPDIAVINN IEFDHADIFS SLDDIVKSFR QFIALIPSNG LLIVNGHDTI ASEISSQAFC
PVERFGMSEA FEWSVSDIDV SETETSFQLA HKGNIAGTIR IDQFGSHTIL NTVAAVAAAS
HAGIPFPVIA EGVRSFKRPK RRMEIVGEFD NGITLIDDFA HHPTAISATL SSLRQRFPER
RILACFEPRS NTSTRNIFQK DLENSFSDAD IVIIGKVHRP ERYAEHERLD TQKLCSSLAG
SGKKVFQSGK DPAGYPEDIV RFIHENIRPD DLIILLSNGS FNGLKTSLTE SFLKKG
//
