MRAY_BORRA
ID MRAY_BORRA Reviewed; 351 AA.
AC B5RRC2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=BRE_310;
OS Borrelia recurrentis (strain A1).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=412418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH94556.1; -; Genomic_DNA.
DR RefSeq; WP_012538808.1; NC_011244.1.
DR AlphaFoldDB; B5RRC2; -.
DR SMR; B5RRC2; -.
DR EnsemblBacteria; ACH94556; ACH94556; BRE_310.
DR KEGG; bre:BRE_310; -.
DR HOGENOM; CLU_023982_0_0_12; -.
DR OMA; LMSPLHH; -.
DR OrthoDB; 1151822at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000612; 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 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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_1000090597"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 88..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"
SQ SEQUENCE 351 AA; 39539 MW; 448F6DD2C1F5A568 CRC64;
MFCFLGLRLL KYITFRTAYA TIFAFLLALI FGPFIISRLK KLKLDQILRK DGPKHHLSEK
MGIPTMGGVL IFFCVLVSLF FWIHFFNIYF LIVLFVMVSF ACLGFTDDLL KIKRKNSDGL
NPKFKIYGQI LFSFISVVML YYFGGEHVSI LYFPFFKSLK LDLGILYIPF GMFVLISASN
SFNLTDGLDG LAIGLSIVVI GALIIIAYLT SRVDFALYLN IPNVKGCEEL VIFLGALLGG
SFGFLWFNAY PAKIMMGDTG SLSIGAVLGM VALILKSEIL FAILAGVFVV ETLSVIIQVV
VYKKTKKRVF KMAPLHHHFE ELGWSEMQVV IRFWIIGLIF AILALSTIKI R
