MRAY_BARBK
ID MRAY_BARBK Reviewed; 356 AA.
AC A1UTC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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};
GN OrderedLocusNames=BARBAKC583_0950;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) 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; CP000524; ABM44543.1; -; Genomic_DNA.
DR RefSeq; WP_005767435.1; NC_008783.1.
DR AlphaFoldDB; A1UTC8; -.
DR SMR; A1UTC8; -.
DR STRING; 360095.BARBAKC583_0950; -.
DR EnsemblBacteria; ABM44543; ABM44543; BARBAKC583_0950.
DR KEGG; bbk:BARBAKC583_0950; -.
DR PATRIC; fig|360095.6.peg.921; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_0_5; -.
DR OMA; LMSPLHH; -.
DR OrthoDB; 1151822at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000643; 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..356
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_1000002938"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ SEQUENCE 356 AA; 38721 MW; 3B3A0FE407101B99 CRC64;
MMLFFSSLYD WLPGVNVFRY ITFRTVAAML TSGLIVFLFG PSIISSLKVR QGKGQPIRAD
GPQTHFKKAG TPTMGGLMIL SGVVISALLW GNLFNIYLWV SLFVMLFFGA IGFYDDYLKV
TKQTDKGFSG KARLSLEFLV ASIASFIILQ VGSPGLALPF VKEYFINLGW FFIPFSACVV
VGLGNAVNLT DGLDGLAIVP VMVASLSFAL IAYLSGNINF ADYLQIHYVS GVGELAVLLG
AVFGAGLGFL WFNAPPAAIF MGDTGSLALG GLLGIVSVAT KHEIVLIFIG GLFVLETLSV
IIQVGWFKLT KKRVFLMAPI HHHFEKKGWT ESQIVVRFWI IAIVLALIGL STLKLR
