ID MRAY_SYNPX Reviewed; 368 AA.
AC Q7U3B6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 71.
DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase;
DE EC=2.7.8.13;
DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase;
GN Name=mraY; OrderedLocusNames=SYNW2516;
OS Synechococcus sp. (strain WH8102).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Synechococcus.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L.,
RA Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J.,
RA Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
CC -!- FUNCTION: First step of the lipid cycle reactions in the
CC biosynthesis of the cell wall peptidoglycan (By similarity).
CC -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
CC D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-
CC Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BX569695; CAE09031.1; -; Genomic_DNA.
DR RefSeq; NP_898605.1; NC_005070.1.
DR STRING; 84588.SYNW2516; -.
DR EnsemblBacteria; CAE09031; CAE09031; SYNW2516.
DR GeneID; 1731045; -.
DR KEGG; syw:SYNW2516; -.
DR PATRIC; 23836827; VBISynSp27240_2682.
DR eggNOG; COG0472; -.
DR HOGENOM; HOG000275124; -.
DR KO; K01000; -.
DR OMA; RFWIVTM; -.
DR ProtClustDB; PRK00108; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:HAMAP.
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:EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 PANTHER; PTHR22926:SF3; PTHR22926:SF3; 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;
KW Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW Membrane; Peptidoglycan synthesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 368 Phospho-N-acetylmuramoyl-pentapeptide-
FT transferase.
FT /FTId=PRO_0000108915.
FT TRANSMEM 11 31 Helical; (Potential).
FT TRANSMEM 42 62 Helical; (Potential).
FT TRANSMEM 88 108 Helical; (Potential).
FT TRANSMEM 112 132 Helical; (Potential).
FT TRANSMEM 152 172 Helical; (Potential).
FT TRANSMEM 180 200 Helical; (Potential).
FT TRANSMEM 211 231 Helical; (Potential).
FT TRANSMEM 237 257 Helical; (Potential).
FT TRANSMEM 265 285 Helical; (Potential).
FT TRANSMEM 293 313 Helical; (Potential).
FT TRANSMEM 346 366 Helical; (Potential).
SQ SEQUENCE 368 AA; 38820 MW; F7CF22E7068D70AC CRC64;
MTDISNRPRT WWENGTVSAS LLAVAVLAGS LASDKWVPNS QLTLPLLIST SVAALVAAAG
IPRLKALKMG QVIRVEGPQA HQSKAGTPTM GGLLVVPVGT IVGGLISLEG TEAQQLLAVS
AITLGYMVIG GFDDWRSLTR QTNTGLTPRG KLLLQSLMGV LFLAVAAWQG WISSSVSLPF
GWTLPLGWLI WPLGLFVFLA ESNATNLTDG LDGLASGCGA LVFLGMAVQL MLRGHTGDPA
LAGFCMTMAG AWLGFLMHNR HPARAFMGDT GSLAMGAALS GVALLSDSLW PLLVMGGVFL
AESLSVIIQV WVFKTTKGPD GQGRRVFRMA PLHHHFELGG TSERTVVPCF WLATAGFVLL
GLLLRPTI
//
