ID A0A2K4ZNM3_9FIRM Unreviewed; 321 AA.
AC A0A2K4ZNM3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000313|EMBL:SOY32083.1};
DE EC=2.7.8.13 {ECO:0000313|EMBL:SOY32083.1};
GN Name=mraY_2 {ECO:0000313|EMBL:SOY32083.1};
GN ORFNames=AMURIS_04836 {ECO:0000313|EMBL:SOY32083.1};
OS Acetatifactor muris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetatifactor.
OX NCBI_TaxID=879566 {ECO:0000313|EMBL:SOY32083.1, ECO:0000313|Proteomes:UP000236311};
RN [1] {ECO:0000313|EMBL:SOY32083.1, ECO:0000313|Proteomes:UP000236311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP69 {ECO:0000313|EMBL:SOY32083.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; OFSM01000038; SOY32083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4ZNM3; -.
DR OrthoDB; 9805475at2; -.
DR Proteomes; UP000236311; Unassembled WGS sequence.
DR GO; GO:0016020; C: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-EC.
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 InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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 PROSITE; PS01348; MRAY_2; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SOY32083.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 321 AA; 34849 MW; 58E6468BAC5FB91B CRC64;
MLYAVVSEKY SSLLALGGIL FAFVATVVAT VKLESHLPKD AGREFAHDGK LSAGKPRGAG
IIFVLAFTAA ALLFTPLKAE IIIYLILIVI CMMTGFLDDA SKMPWGEFRK GFLDLCVAAL
TAMTFLKYNS NAIELAFFHM GIVIPKGLFA VLAVILVWVS VNVTNCSDGV DGLSGTLAII
SMTTIYLVDR ILEAGQDFSF LILLFAACIL GYLWYNATPS RLLMGDAGSR AMGLFISIAV
LKTGRPLLYI PVALVLILDG GLGLIKVSLL RMGKIRILKK VRTPLHDHVR KIWGWSNTQT
VFRFAIIQII LAVAVVYGIG M
//
