ID B1X4H1_PAUCH Unreviewed; 368 AA.
AC B1X4H1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Phospho-N-acetylmuramoyl-pentapeptidetransferase {ECO:0000313|EMBL:ACB42840.1};
GN Name=mraY {ECO:0000313|EMBL:ACB42840.1};
GN OrderedLocusNames=PCC_0400 {ECO:0000313|EMBL:ACB42840.1};
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore {ECO:0000313|EMBL:ACB42840.1}.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717 {ECO:0000313|EMBL:ACB42840.1};
RN [1] {ECO:0000313|EMBL:ACB42840.1}
RP NUCLEOTIDE SEQUENCE.
RA Gloeckner G., Nowack E., Melkonian M.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB42840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000256|ARBA:ARBA00005583}.
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DR EMBL; CP000815; ACB42840.1; -; Genomic_DNA.
DR RefSeq; YP_002049050.1; NC_011087.1.
DR AlphaFoldDB; B1X4H1; -.
DR GeneID; 6481810; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
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 NCBIfam; TIGR00445; mraY; 1.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF5; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR Pfam; PF10555; MraY_sig1; 1.
DR PROSITE; PS01347; MRAY_1; 1.
DR PROSITE; PS01348; MRAY_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plastid {ECO:0000313|EMBL:ACB42840.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACB42840.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 368 AA; 39752 MW; CE5669B7C24AD3E9 CRC64;
MNNSPLTNKT NETRFSGKFA SAILISFIIT TFVIIDILIP DSTLTIPLVA SAVISGSICN
WFIPLLSSLK MGQIIRIDGP ISHYSKANTP TMGGLLIIPV GVVVGNLFTL GMISHERIIV
LGAIILSYMV IGSIDDLQSL NQNINTGLLP HQKIKLQSIA AILFMVWASW FGWISTDIAL
PSVQILSIKL LIWPLALFVF LAESNATNLT DGLDGLAAGC STLVFSGLTI QLILRGNLDD
TNLASFCAAM TGSWLGFLTL NRNPARIFMG DAGSLALGAG ITGIALISNN LWPLLLTGGI
FLIESICVIM QVAIFRVTRK ITGKGKRLFE MAPLHHHFEL RGVKEEIIVL AFWLVSLFLA
VTSLLPIP
//
