ID   MURF_BORBU              Reviewed;         464 AA.
AC   Q44777; O51284;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=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; OrderedLocusNames=BB_0304;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-464.
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RA   Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; AE000783; AAC66644.1; -; Genomic_DNA.
DR   EMBL; U43739; AAA85627.1; -; Genomic_DNA.
DR   PIR; H70137; H70137.
DR   RefSeq; NP_212438.1; -.
DR   GeneID; 1195141; -.
DR   GenomeReviews; AE000783_GR; BB_0304.
DR   KEGG; bbu:BB0304; -.
DR   NMPDR; fig|224326.1.peg.688; -.
DR   TIGR; BB_0304; -.
DR   HOGENOM; Q44777; -.
DR   OMA; Q44777; VEGNEEY.
DR   BioCyc; BBUR224326:BB_0304-MON; -.
DR   BRENDA; 6.3.2.10; 142596.
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; 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; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    464       UDP-N-acetylmuramoyl-tripeptide--D-
FT                                alanyl-D-alanine ligase.
FT                                /FTId=PRO_0000101695.
FT   NP_BIND     125    131       ATP (Potential).
FT   CONFLICT    462    464       IFR -> YI (in Ref. 2; AAA85627).
SQ   SEQUENCE   464 AA;  53446 MW;  29038B0C533799BC CRC64;
     MRIKIKDILI SSKDVKFVGN IKNIERVVSF YSLDSREIKD DNINDSLYFA YKGNKVDGFS
     FVKYLIDLGV KCFACSREHE SECIKYLNDN EGLVFLLTSN VIKLLQALAS FLIEKTSFKR
     IAITGSNGKT TTKEMLYSIL SKKYKTYKTW GNLNSDIGLP LSILRVEGNE EYAVFEVGVS
     YVGEMDLLSQ ILKPEIVIIT NISYAHMQAF KELQAIAFEK SKIIGKNIEI FVVNEMNDYC
     VYLEKRAKIA NPNVKIVYFD FENLSIKSFS FLDGKFSFDF VYKGFEYSIL LLGRHNIFNA
     IGCINLALFL GMREKEIKEG LIETAFQKGR AEILTKNGYL ILNDSYNGNM GSFMALKNMI
     LDLNIQNKKF IVLGSFKELG ELAYKTHKDL IQEAISMNFD KIFLIGEEFL DVRDSENLVE
     KCLYYFSEFD KFIDFFLKSL EPSVFIVIKG SRFNRLERIL NIFR
//