MRAY_BORBU
ID MRAY_BORBU Reviewed; 351 AA.
AC Q44776; Q60120;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038};
DE EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038};
DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; OrderedLocusNames=BB_0303;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX 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., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-351.
RC STRAIN=212;
RA Ge Y., Old I.G., Saint-Girons I., Charon N.W.;
RT "Mapping and sequencing of a locus involved in the cell division of
RT Borrelia burgdorferi.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the initial step of the lipid cycle reactions in
CC the biosynthesis of the cell wall peptidoglycan: transfers
CC peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-
CC pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding
CC undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
CC {ECO:0000255|HAMAP-Rule:MF_00038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-
CC alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC alanyl-D-alanine + UMP; Xref=Rhea:RHEA:28386, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:61386, ChEBI:CHEBI:61387; EC=2.7.8.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00038};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00038};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00038}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00038}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
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DR EMBL; U43739; AAA85626.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66645.1; -; Genomic_DNA.
DR EMBL; X96685; CAA65460.1; -; Genomic_DNA.
DR EMBL; X96432; CAA65292.1; -; Genomic_DNA.
DR PIR; G70137; G70137.
DR RefSeq; NP_212437.1; NC_001318.1.
DR RefSeq; WP_002556902.1; NC_001318.1.
DR AlphaFoldDB; Q44776; -.
DR SMR; Q44776; -.
DR STRING; 224326.BB_0303; -.
DR DNASU; 1195140; -.
DR EnsemblBacteria; AAC66645; AAC66645; BB_0303.
DR GeneID; 56567734; -.
DR KEGG; bbu:BB_0303; -.
DR PATRIC; fig|224326.49.peg.702; -.
DR HOGENOM; CLU_023982_0_0_12; -.
DR OMA; LMSPLHH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase 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 CDD; cd06852; GT_MraY; 1.
DR HAMAP; MF_00038; MraY; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR Pfam; PF10555; MraY_sig1; 1.
DR TIGRFAMs; TIGR00445; mraY; 1.
DR PROSITE; PS01347; MRAY_1; 1.
DR PROSITE; PS01348; MRAY_2; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..351
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_0000108790"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT CONFLICT 91
FT /note="L -> C (in Ref. 3; CAA65460/CAA65292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39480 MW; F6FE800C0C6151E3 CRC64;
MFYLLGLRLL KYITFRMAYA TIFAFLLSLI VGPYIILKLK KLRADQILRE DGPKRHLSEK
AGIPTMGGIL IFFCVFISLV FWSNILNVYF LIMVFVMLGF AFLGFIDDFL KIKKKTSDGL
KARFKIYGQI IFSFFSVGIL YYFGGEHVSV IYFPFIKSFQ IDLGLFYIPF GMFILISASN
SFNLTDGLDG LAIGLSIVIT GALIIIAYLT SRADFAAYLH IPNIKGSEEL VIFLGALLGG
SFGFLWFNAY PAKIMMGDTG SLALGAILGM AALILKSEIL FSILAGVFII ETMSVIIQVL
VYKKTKKRVF KMAPLHHHFE ELGWSEMQVV IRFWIIGLIF AIIALSTIKI R
