MURF_SYNY3
ID MURF_SYNY3 Reviewed; 454 AA.
AC P45450; P74091;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019};
DE EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019};
DE AltName: Full=UDP-MurNAc-pentapeptide synthetase;
GN Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; OrderedLocusNames=slr1351;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7894708; DOI=10.1099/00221287-141-1-163;
RA Malakhov M.P., Los D.A., Wada H., Semenenko V.E., Murata N.;
RT "Characterization of the murF gene of the cyanobacterium Synechocystis sp.
RT PCC 6803.";
RL Microbiology 141:163-169(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC murein. {ECO:0000255|HAMAP-Rule:MF_02019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02019};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02019}.
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DR EMBL; X62437; CAA44303.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18171.1; -; Genomic_DNA.
DR PIR; S75610; S75610.
DR AlphaFoldDB; P45450; -.
DR SMR; P45450; -.
DR IntAct; P45450; 1.
DR STRING; 1148.1653256; -.
DR PaxDb; P45450; -.
DR EnsemblBacteria; BAA18171; BAA18171; BAA18171.
DR KEGG; syn:slr1351; -.
DR eggNOG; COG0770; Bacteria.
DR InParanoid; P45450; -.
DR OMA; VEMGANH; -.
DR PhylomeDB; P45450; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
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-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_02019; MurF; 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 InterPro; IPR005863; UDP-N-AcMur_synth.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR SUPFAM; SSF63418; SSF63418; 1.
DR TIGRFAMs; TIGR01143; murF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..454
FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT ligase"
FT /id="PRO_0000101706"
FT BINDING 116..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
FT CONFLICT 290
FT /note="L -> V (in Ref. 2; BAA18171)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="D -> A (in Ref. 2; BAA18171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 48297 MW; 05FABDB6A3D29723 CRC64;
MNSKLSLFDI RTFLESCLLS VTNLSEDIRI NNICTDTRSL VSGDLFLALR GESFDGHSFI
PQALTAGAIA VVTDRPVEGL GETVAQFLVE DTLVAYQHIA AGWRQRFTIP IIGVTGSVGK
TTTKELIAAV LSQFGNVHKT RANYNNEIGV PKTLLELSPD HDFAIVEMAM RGRGQIALLA
DIAKPTIGLI TNVGTAHIGL LGSELAIAEA KCELLAHQPP ESTAILNRDN ALLMETAQRF
WQGKTITYGL EGGDVHGTVD GENLILDGVS LPLPLAGVHN ASNYLAAIAL AQCLGLDWQQ
LQSGLTVELP KGRARRYQWG QDVVLLDETY NDGLESMLAS LDLLANTPGK RRLAVLGAMK
ELGDYGPTFH QRVGAKVKAL GLDGLFLLAN DPNTDAIAAG ANGVETQSFS DGPSLVAALK
TTLQPGDRLL FKASNSVGLG AVVSQLLAEN PTSV
