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MRAY_ANOFW
ID   MRAY_ANOFW              Reviewed;         324 AA.
AC   B7GGI5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Aflv_1833;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(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 membrane {ECO:0000255|HAMAP-Rule:MF_00038};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000922; ACJ34194.1; -; Genomic_DNA.
DR   RefSeq; WP_012575392.1; NC_011567.1.
DR   AlphaFoldDB; B7GGI5; -.
DR   SMR; B7GGI5; -.
DR   STRING; 491915.Aflv_1833; -.
DR   EnsemblBacteria; ACJ34194; ACJ34194; Aflv_1833.
DR   KEGG; afl:Aflv_1833; -.
DR   PATRIC; fig|491915.6.peg.1885; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_0_1_9; -.
DR   OMA; LMSPLHH; -.
DR   OrthoDB; 1151822at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000742; 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 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..324
FT                   /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT                   /id="PRO_1000116502"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ   SEQUENCE   324 AA;  35437 MW;  D4DC3F59D318378D CRC64;
     MNEKVILFTA GLAFIITVVL SPIFIPFLRR LKFGQSIREE GPKSHQKKSG TPTMGGLMIL
     LSLSITTWLM SDIFFERTAH TYMLLFVTVG YGLLGFIDDF IKVVMKRNLG LTSKQKLAGQ
     LLIALIFYFF FQHYSMSTVV SIPGTDVSLD LGVAYVLLII FMLVGGSNAV NLTDGLDGLL
     AGTAAIAFGA YAVLAWNQGQ YDVAIFSVAV VGAVLGFLVF NAHPAKVFMG DTGSLALGGA
     IVTIAILTKL EILLVIIGGV FVIETLSVII QVISFKTTGK RVFRMSPLHH HYELIGWSEW
     RVVVTFWAVG LLFAILGIYI EVWV
 
 
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