ID A0A0N7HX49_9BACT Unreviewed; 460 AA.
AC A0A0N7HX49;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:ALJ01057.1};
GN ORFNames=DC20_21250 {ECO:0000313|EMBL:ALJ01057.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ01057.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALJ01057.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALJ01057.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012643; ALJ01057.1; -; Genomic_DNA.
DR RefSeq; WP_062545694.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0N7HX49; -.
DR STRING; 512763.DC20_21250; -.
DR KEGG; rti:DC20_21250; -.
DR PATRIC; fig|512763.3.peg.4668; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000061382; Chromosome.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000061382}.
FT DOMAIN 8..107
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 114..288
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 312..358
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 460 AA; 52130 MW; 778517BCD5AED4E5 CRC64;
MSTEAYQHIH MIAIGGSIMH NLALALHRKG LKVTGSDDEI FEPAKGRLAA EGLLPEAEGW
FPEKLHSTPD AVIVGMHARP DNPELLYAQE HNIPIFSFPE FIYEQSKNKQ RIVIAGSHGK
TSITSIILHV LKYHNRLFDY AVGAQLEGFD LMVKLTEEAP IIVIEGDEYL SSPIQRVPKI
HKYHHHIGVI SGISWDHINV FPTEENYREQ FRIFVDMTPK AGTLIYNQDD EQVQEVCVPN
NSDVNYIGYT IHEHKIKKSG KTVLKTKKDD VEIQLFGEHN LRNISAAKEV CKQIGIKGQA
FYEALATFKG AARRLEKIGE NEHTLVYKDF AHAPSKLKAT SEALKKQFPD RQLIACLELH
TFSSLNKDFL PQYKGTFLSP DVKIVYFNPK TLEHKRMPPL DPQDLKAAFG DENIEVYTDN
QALQEYLLNN NWKDKNLLMM TSGNFGNLDL QKLADTITAS
//
