ID   MURF_RICMO              Reviewed;         449 AA.
AC   Q9AKP1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Probable UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE            EC=6.3.2.10;
DE   AltName: Full=UDP-MurNAc-pentapeptide synthetase;
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme;
GN   Name=murF;
OS   Rickettsia montana.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=33991;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21219194; PubMed=11319266;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes.";
RL   Mol. Biol. Evol. 18:829-839(2001).
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final
CC       step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
CC       precursor of murein (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-
CC       glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-
CC       acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC       alanine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; AJ293315; CAC33607.1; -; Genomic_DNA.
DR   HSSP; P11880; 1GG4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-...; IEA:EC.
DR   GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-d...; 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:0007047; 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   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005863; UDP-N-AcMur-3pep_AlaAla_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   PANTHER; PTHR23135:SF3; MurF; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 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;
KW   Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    449       Probable UDP-N-acetylmuramoyl-
FT                                tripeptide--D-alanyl-D-alanine ligase.
FT                                /FTId=PRO_0000259657.
FT   NP_BIND     106    112       ATP (Potential).
SQ   SEQUENCE   449 AA;  50322 MW;  59FDCF74127534A0 CRC64;
     MIWNSKTLSA ALGITISNSI NCNEVQFNSK DVKKGDLFIA LQGNRDGHDY VLDAIDKGAA
     AVIISKQVEI NDKDKIILVD DCFEALQKMA LYKRENSKAK FIVITGSVGK TSTKEALKVL
     LQHDFLVFAS RGNFNNKLGM LINLASMADD TEYAIFELGM NHKGEIRELV QILKPNIAMI
     TNISEAHLEF FNSLEEIAEA KCEIFANFSK NDIAVINADT NCYNKILSIL KNLSITDIHS
     FGRSSKTSAE LILYENLGEQ VYLKYKINNK VLDVTIPFIP RHFTENYTGV LLIIDILGKD
     IEIAANHLAN ISPTKGRGEI INIQNCRVIC DYYNASPQSM KAALEYLKQV PAENKTAIIG
     DMLELGENSK RLHEKLVQYI LDAACSKVYL VGVNTKYIDD LLPSKIAKKY FKNVDELMTH
     ITDLFEGNEL ILIKGSRGVK LDKIVDYYK
//