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Database: UniProt
Entry: U2PMK3_9FIRM
LinkDB: U2PMK3_9FIRM
Original site: U2PMK3_9FIRM 
ID   U2PMK3_9FIRM            Unreviewed;       359 AA.
AC   U2PMK3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Putative ATP synthase F0, A subunit {ECO:0000313|EMBL:ERK45371.1};
GN   ORFNames=HMPREF0367_01064 {ECO:0000313|EMBL:ERK45371.1};
OS   Faecalitalea cylindroides ATCC 27803.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalitalea.
OX   NCBI_TaxID=649755 {ECO:0000313|EMBL:ERK45371.1, ECO:0000313|Proteomes:UP000016658};
RN   [1] {ECO:0000313|EMBL:ERK45371.1, ECO:0000313|Proteomes:UP000016658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27803 {ECO:0000313|EMBL:ERK45371.1,
RC   ECO:0000313|Proteomes:UP000016658};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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}.
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:ERK45371.1}.
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DR   EMBL; AWVI01000043; ERK45371.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2PMK3; -.
DR   PATRIC; fig|649755.3.peg.986; -.
DR   HOGENOM; CLU_023982_2_4_9; -.
DR   OrthoDB; 9783652at2; -.
DR   Proteomes; UP000016658; 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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   CDD; cd06853; GT_WecA_like; 1.
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:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   359 AA;  39432 MW;  D5B487C5B59A4063 CRC64;
     MLIVPFFISL GLTPLIKKYS VIAKTYAKEN ERTIHHGKIS RIGGVAIYVS FIISMALFVK
     ADMAVNGMIL GGSLMFFAGL IDDLIDMKPL VKLAFEVCAA FILVAFGVGV DVLRLPFGIT
     IDSIALSIVF TIIWIVGITN AVNLIDGLDG LCGGMSVVIF VVIGCIAIVE RRMDITIITF
     LLAASIFGFL VYNAHPASIF MGDCGSLFLG FMISAISLLG FKSSTIVTLA LPMLLLMLPI
     IDTLSAILRR TLKGRKFLEA DKSHIHHLLM KQFGHRNTVI IMCGITTLFG FSAFVYMLNE
     MFGLLAIMII LLAVEIFIEK SAMISEHFHP ILGICRRGLN RIKLITKIIK EHKEKKSAK
//
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