ID Q72JQ4_THET2 Unreviewed; 438 AA.
AC Q72JQ4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamyl-L-ornithine-D-alanyl-D-alanine ligase {ECO:0000313|EMBL:AAS81062.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:AAS81062.1};
GN OrderedLocusNames=TT_C0714 {ECO:0000313|EMBL:AAS81062.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS81062.1, ECO:0000313|Proteomes:UP000000592};
RN [1] {ECO:0000313|EMBL:AAS81062.1, ECO:0000313|Proteomes:UP000000592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27
RC {ECO:0000313|Proteomes:UP000000592};
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Overbeek R., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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DR EMBL; AE017221; AAS81062.1; -; Genomic_DNA.
DR RefSeq; WP_011173153.1; NZ_CP133179.1.
DR AlphaFoldDB; Q72JQ4; -.
DR KEGG; tth:TT_C0714; -.
DR eggNOG; COG0770; Bacteria.
DR HOGENOM; CLU_031507_1_1_0; -.
DR OrthoDB; 9801978at2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.40.1390.10; MurE/MurF, N-terminal 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 InterPro; IPR035911; MurE/MurF_N.
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; PF01225; Mur_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.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 4: Predicted;
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:0000313|EMBL:AAS81062.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 48..92
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..285
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 306..370
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 438 AA; 46688 MW; 6A4991B6D599BA36 CRC64;
MLKGGEDVVQ GTHVRELTPE WVARAVGGRL HPGGGPVRDL VWHSGAATPG SLFAALPGRT
THGRHFIPEA LARGASLVLA DQAGPATLEV EDPWQALLRL GEALRRLFPG PVLAVGGSSG
KTTTKEALAQ GLGLPAPPGN LNTAPPLVRF FWHLDPQSPG AVVELGVDRQ GEMAELFALA
KPHLAVLTAL GEEHLEAFGT LEKAVQEEAH LLRAPTALVG EQAAPLVLGL REDLLVYGFA
EGTFRGRDLE LGLRESRFRY GGLHVRVPYP GLGPAYGALA ALAAAEVLGL SLEEVAERLS
RLTLPPGRME TREVGGVVFV NDAYNANPLS VKAGLRWLAA QPGRKWAVLG EMRELGRESL
RLHLEVAEEA ARLGLSPLYL GPHARHQAAF SGEAVESLEE ALAWLKARVA PGDLVYLKAS
RAVGLERIVE LWDAPFSS
//
