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Database: UniProt
Entry: A0A1Y2PAD3_9FLAO
LinkDB: A0A1Y2PAD3_9FLAO
Original site: A0A1Y2PAD3_9FLAO 
ID   A0A1Y2PAD3_9FLAO        Unreviewed;       408 AA.
AC   A0A1Y2PAD3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=WH52_11115 {ECO:0000313|EMBL:OSY87423.1};
OS   Tenacibaculum holothuriorum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1635173 {ECO:0000313|EMBL:OSY87423.1, ECO:0000313|Proteomes:UP000194221};
RN   [1] {ECO:0000313|EMBL:OSY87423.1, ECO:0000313|Proteomes:UP000194221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2-2 {ECO:0000313|EMBL:OSY87423.1,
RC   ECO:0000313|Proteomes:UP000194221};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Tenacibaculum sp. S2-2, isolated from intestinal
RT   microbiota of sea cucumber, Apostichopus japonicas.";
RL   Submitted (MAR-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00038};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00038,
CC         ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00038}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000256|ARBA:ARBA00005583, ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSY87423.1}.
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DR   EMBL; LAPZ01000011; OSY87423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2PAD3; -.
DR   STRING; 1635173.WH52_11115; -.
DR   InParanoid; A0A1Y2PAD3; -.
DR   OrthoDB; 9805475at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000194221; Unassembled WGS sequence.
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   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   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell division {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   Magnesium {ECO:0000256|HAMAP-Rule:MF_00038, ECO:0000256|PIRSR:PIRSR600715-
KW   1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00038};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00038,
KW   ECO:0000256|PIRSR:PIRSR600715-1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194221};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00038};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00038}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        75..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        98..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        136..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        213..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        242..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        281..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        332..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   TRANSMEM        386..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   408 AA;  45449 MW;  9AE99FCB5A600940 CRC64;
     MLYYLFEYLE SEFNLTGASV FQFITFRSAA AFIISLLIST IFGKRIINFL RRQQVGETVR
     DLGLEGQIQK AGTPTMGGII IILATLVPVL LFAKLENIYI IILLITTVWM GLIGFADDYI
     KVFKKDKEGL KGRFKVLGQV GLGVIVGSML YFHPDVTIKE QLPENQQVVQ ANERKQVFGD
     AHKSTKTTVP FLKDNELDYA KALSFLGDDY KKYAWLIFIP FVIFIITAVS NGANLTDGID
     GLAAGSSAII VIALAIFAWV SGNIIFADYL DVMYIPKSGE MTVFILAFAG ALIGFLWYNT
     YPAQVFMGDT GSLTIGGIIA VIAIAIRKEL LIPVLAGVFL AENLSVMLQV SYFKYTKKKY
     GEGRRIFKMS PLHHHYQKSG YHESKIVTRF WIVGILLAVL AIVTLKLR
//
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