ID W0RM66_9BACT Unreviewed; 505 AA.
AC W0RM66;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:AHG91557.1};
GN ORFNames=J421_4020 {ECO:0000313|EMBL:AHG91557.1};
OS Gemmatirosa kalamazoonensis.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91557.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG91557.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG91557.1,
RC ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
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DR EMBL; CP007128; AHG91557.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RM66; -.
DR STRING; 861299.J421_4020; -.
DR KEGG; gba:J421_4020; -.
DR PATRIC; fig|861299.3.peg.4077; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_0_2_0; -.
DR InParanoid; W0RM66; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000019151; 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, ECO:0000313|EMBL:AHG91557.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT DOMAIN 24..123
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 131..323
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 344..407
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 505 AA; 54436 MW; 6CD5E8F76155104A CRC64;
MSTTTTPAPN GNVLETIDGA SVRRIHLLGV AGTGMGAFAG MLKAAGYDVT GSDTNVYPPM
SDMLRAWEID VMTPYDPANL DRARPDLVIV GNVIRRENPE ATAVRERGLP SMSFPAAFGS
LILATRHSVV VAGTHGKTTT SALMAHVLAA AGLDPTFLVG GVTRNYDSNF RLGKGPHAVV
EGDEYDTAYF DKGPKFMHYR ARTAILTSLE FDHADIYRDL PHYESAFERF AAVVPPEGQL
IVSAQYPRLV AIARAHGEAP VVTYAAAPHE VPDTRFQAVD VRLGPDGARF RVRDAERGST
SPEYHLPMAG YHNVENAVGV YVAARALGLT DEQIAPGFAT FAGVKRRQEP RGEIGGVLVL
DDFAHHPTAV RETVAAVRAR YPDRRLLAVF EPRSNTSRRN LHQAEYGEAF EGAQHVFLRE
PEPHDKVPVD QRLDAHAVVR ALEAHGIEAE VHEPVPTLVQ CVADTAAPGD VVLVMSNGAF
GGFIPSLLDA LASRAARRAQ DAPNG
//
