(data stored in ACNUC7421 zone)

SWISSPROT: A4ATM0_MARSH

ID   A4ATM0_MARSH            Unreviewed;       406 AA.
AC   A4ATM0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   16-JAN-2019, entry version 78.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000256|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000256|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000256|HAMAP-Rule:MF_00038};
GN   OrderedLocusNames=FB2170_16936 {ECO:0000313|EMBL:EAR00790.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00790.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00790.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: First step of the lipid cycle reactions in the
CC       biosynthesis of the cell wall peptidoglycan. {ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-
CC         alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC         alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol + UMP;
CC         Xref=Rhea:RHEA:21920, ChEBI:CHEBI:57865, ChEBI:CHEBI:60032,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:70758; EC=2.7.8.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00038};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00038}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00038}.
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DR   EMBL; CP002157; EAR00790.1; -; Genomic_DNA.
DR   RefSeq; WP_013304593.1; NC_014472.1.
DR   STRING; 313603.FB2170_16936; -.
DR   EnsemblBacteria; EAR00790; EAR00790; FB2170_16936.
DR   KEGG; fbc:FB2170_16936; -.
DR   eggNOG; ENOG4105CPY; Bacteria.
DR   eggNOG; COG0472; LUCA.
DR   HOGENOM; HOG000275122; -.
DR   KO; K01000; -.
DR   OMA; LMSPLHH; -.
DR   OrthoDB; 1151822at2; -.
DR   BioCyc; MSP313603:G1GNS-165-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001602; 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: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;
DR   PRODOM; A4ATM0.
DR   SWISS-2DPAGE; A4ATM0.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00038,
KW   ECO:0000313|EMBL:EAR00790.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00038}.
FT   TRANSMEM     20     43       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM     75     92       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM     98    116       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    136    153       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    211    228       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    240    264       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    270    296       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    303    324       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    330    353       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    384    403       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
SQ   SEQUENCE   406 AA;  45157 MW;  536844A8A16EDEF0 CRC64;
     MLYYLFEYLE NEYQVPGASL FGFTTFRAAM AILFSLLLAT VYGKKVILFL QRKQIGESIR
     DLGLDGQKQK AGTPTMGGLI IIMATLIPVL LFADIMNIYI ILLIVTILWM GTIGFIDDYI
     KIFKKDKAGL KGRFKILGQV VLGLIVGATL YFHPEVTMRE HDKSIITEQY TVEQVKGEDI
     KSTRTTVPFI KNNEFDYGNL ISWAGDGAKD YVWLIFVPMI ILIVTAVSNG ANLTDGIDGL
     AAGTSAIIVF TLGVFTWVSG NIIFSDYLDI MYITGVGELL VFVTAFVGAL VGFLWYNAFP
     ATVFMGDTGS LTIGGVIAVI AIIIRKELLI PILCGIFFAE SISVMLQVGY FKYTKKKLGE
     GKRIFLMAPL HHHYQKKGYH ESKIVTRFWI VGILLAIITI VTLKVR
//

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