ID E6X0N7_NITSE Unreviewed; 353 AA.
AC E6X0N7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=Nitsa_0487 {ECO:0000313|EMBL:ADV45757.1};
OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Nitratifractor.
OX NCBI_TaxID=749222 {ECO:0000313|EMBL:ADV45757.1, ECO:0000313|Proteomes:UP000008633};
RN [1] {ECO:0000313|EMBL:ADV45757.1, ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RX PubMed=21886859;
RA Anderson I., Sikorski J., Zeytun A., Nolan M., Lapidus A., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Ngatchou-Djao O.D., Rohde M., Tindall B.J., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-
RT 1).";
RL Stand. Genomic Sci. 4:322-330(2011).
RN [2] {ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nitratifractor salsuginis DSM 16511.";
RL Submitted (JAN-2011) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00038}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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}.
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DR EMBL; CP002452; ADV45757.1; -; Genomic_DNA.
DR RefSeq; WP_013553453.1; NC_014935.1.
DR AlphaFoldDB; E6X0N7; -.
DR STRING; 749222.Nitsa_0487; -.
DR KEGG; nsa:Nitsa_0487; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_0_7; -.
DR OrthoDB; 9805475at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008633; Chromosome.
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 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 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 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:UP000008633};
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 13..36
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 90..108
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 225..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 256..275
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 353 AA; 38953 MW; 7D7289B2AD846729 CRC64;
MFYYLHEALG IHLFYYISVR AGLAFFIAFC LTLFLMPRYI AWAKARKANQ PINKYVPAHE
EKQHTPTMGG AIFVFSTVIA SLLTAKLNNW YVIGGLLTLV GFAAVGFKDD LGKVLSGDNL
QGLTARGKMA LLILVSLLVS SLLVFVAHFP TTFYVPFIKT PLFDMGYFAI LFWTLVIIAT
SNAVNLTDGL DGLATVPTVI ALGTLGIIVY LTGHAIFSKY LLLPYIPGVG EITIVAAALA
GGLLGFLWYN CYPAEVFMGD TGSLSIGAFL AYMAILGKSE VLLILIGIVF VIETVSVILQ
VGSWKLRQKR VFLMAPIHHH FEMKKWAENK IIVRFWMVAF LANLLALITL KIR
//
