ID J3CWV6_9BRAD Unreviewed; 459 AA.
AC J3CWV6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide synthase {ECO:0000313|EMBL:EJN14334.1};
GN ORFNames=PMI42_02104 {ECO:0000313|EMBL:EJN14334.1};
OS Bradyrhizobium sp. YR681.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN14334.1, ECO:0000313|Proteomes:UP000007272};
RN [1] {ECO:0000313|EMBL:EJN14334.1, ECO:0000313|Proteomes:UP000007272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR681 {ECO:0000313|EMBL:EJN14334.1,
RC ECO:0000313|Proteomes:UP000007272};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN14334.1}.
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DR EMBL; AKIY01000083; EJN14334.1; -; Genomic_DNA.
DR RefSeq; WP_008133089.1; NZ_AKIY01000083.1.
DR AlphaFoldDB; J3CWV6; -.
DR PATRIC; fig|1144344.3.peg.1973; -.
DR OrthoDB; 9801978at2; -.
DR Proteomes; UP000007272; Unassembled WGS sequence.
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; 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; 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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 121..294
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 324..371
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 459 AA; 48020 MW; 48F6210CA5C7E926 CRC64;
MSGPIWTVAE VARALGAAGS FPDTPIDFVT QDSRLVKPGS LFVALSGTPS GGFVSAFASA
RDGWEFADKA EASGAVAMIV PHEIAGIKVP QIVVKDTLIG GLWGLARAAR ARFNGPVIGL
TGSAGKTSTK EFLAAYPNAY ASPSSFNNFW GVPLTLCNAR PDASLWVVEM GMNQTGEIAR
LSELTRPTVA LVVNVQPVHL EKLGSLEAIR REKVSIALGL PEDGVLVLPA GLKASEWKGK
VIRFGEKAEV HEVKHAPHGE GWQVLAVIGK KEIAFSLTPG APHRVQNALA ALAAIRAANL
DASTLAIKLD RVGIMTGRGV EQAVGGITVI DDSFNGNPAS VAAALQSLQA RNVSGGRRIA
VLGDMLELGD DAPSYHTALA RHLDGIDGVY CVGPLMRHLY DVLPAGKGLG WHDDPATLKA
GEVANLLKAG DVVVVKGSKK MFWVNKFVPG LVAALQAKA
//