ID   MURF_RICCN              Reviewed;         449 AA.
AC   Q92H60;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=RC0911;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03449.1; -; Genomic_DNA.
DR   PIR; G97813; G97813.
DR   RefSeq; WP_010977511.1; NC_003103.1.
DR   AlphaFoldDB; Q92H60; -.
DR   SMR; Q92H60; -.
DR   EnsemblBacteria; AAL03449; AAL03449; RC0911.
DR   KEGG; rco:RC0911; -.
DR   PATRIC; fig|272944.4.peg.1035; -.
DR   HOGENOM; CLU_031507_1_2_5; -.
DR   OMA; VEMGANH; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000816; 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.
FT   CHAIN           1..449
FT                   /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT                   ligase"
FT                   /id="PRO_0000101703"
FT   BINDING         106..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   449 AA;  50285 MW;  1E06569FB152F281 CRC64;
     MIWNSKTLSA VLGITISNSI SCNEVQFNSK DVKKGNLFIA LQGNRDGHDY VLDAIDKGAA
     AVIISKRVEI NDKDKIILVD DCFEALQKMA LYKRENSKAK FIAITGSVGK TSTKEALKVL
     LQHDFLVFAS RGNFNNKLGM LINLASMADD TEYAIFELGM NHKGEIRELV QILKPNIAMI
     TNISEAHLEF FNSLEEIAEA KCEIFANFSK NDIAVINADT NCYNKILSIL KNLSITDIHS
     FGRSAKTSAE LILYENLGEQ VYLKYKINKK VLDVTIPFIP RHFTENYTGV LLIIDILGKD
     IEIAANHLAN ISPTKGRGEI INIQNCRVIC DYYNASPQSM KAALEYLKQV PAENKTAIIG
     DMLELGENSK RLHEKLVQYI LDAACSKVYL VGVNTKYIND LLPAKIAKKY FKNVDELITH
     ITDLFEGNEL ILIKGSRGVK LDKIVDYYK