ID R9T4I5_METII Unreviewed; 490 AA.
AC R9T4I5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN ORFNames=MMINT_04560 {ECO:0000313|EMBL:AGN25837.1};
OS Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX NCBI_TaxID=1295009 {ECO:0000313|EMBL:AGN25837.1, ECO:0000313|Proteomes:UP000014070};
RN [1] {ECO:0000313|EMBL:AGN25837.1, ECO:0000313|Proteomes:UP000014070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Issoire-Mx1 {ECO:0000313|EMBL:AGN25837.1,
RC ECO:0000313|Proteomes:UP000014070};
RX PubMed=23846268; DOI=10.1128/genomeA.00453-13;
RA Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT human feces.";
RL Genome Announc. 1:142-142(2013).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The
CC heterotrimers can form oligomers, although 1 heterotrimer is thought to
CC be able to translocate proteins. Interacts with the ribosome. May
CC interact with SecDF, and other proteins may be involved.
CC {ECO:0000256|HAMAP-Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|HAMAP-Rule:MF_01465,
CC ECO:0000256|RuleBase:RU004349}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01465}.
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DR EMBL; CP005934; AGN25837.1; -; Genomic_DNA.
DR AlphaFoldDB; R9T4I5; -.
DR STRING; 1295009.MMINT_04560; -.
DR KEGG; mer:MMINT_04560; -.
DR HOGENOM; CLU_031763_3_0_2; -.
DR InParanoid; R9T4I5; -.
DR Proteomes; UP000014070; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR NCBIfam; TIGR00967; 3a0501s007; 1.
DR PANTHER; PTHR10906:SF1; DSEC61ALPHA; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01465};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01465}; Reference proteome {ECO:0000313|Proteomes:UP000014070};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01465}.
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 125..149
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 229..246
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 271..297
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 363..386
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT DOMAIN 8..42
FT /note="Translocon Sec61/SecY plug"
FT /evidence="ECO:0000259|Pfam:PF10559"
SQ SEQUENCE 490 AA; 52632 MW; 774D81BC81B83F1D CRC64;
MWVILMLVLY FIMTNIYLYG LDQSNILDIF GPYRTILAGS QGSLMHLGIG PIVTASIIMQ
LFVGAKIIKL DLTDDQDKSV YQSTQKLLVI VMIIIESVPQ VFGYLTPSPS LVSGLDGVVG
STGLISGGTL AAFIIVLQLC IGSYLVFLMD EVISKWGIGS GISLFIAAGV AEAIFTGTLN
WNSVNGGDLS LSNPPAGTIP KTFYYIFNMS SAQMASGGYE SILLQPPNPM IALIGTIIIF
LFVAYIESSR IELPLAHGAA RGARGRYPIK LLYASNIPVI LMSALLANFS IVSLLLYTNP
TLEGIPLIGH NDWIGMYPDG TTTAEGGLAW YLSTPNGLSG WLLPILDPAQ YGSYAYGHTP
LQVIAKVIIF FGAMVFGSIL FAKFWIMTTN MGPESVARQI ESSGMQIPGF RRDPRVLKRV
LERYIPVVTV LSGAIVGALA AGADLIGTVG NASGTGVLLA VGILIHFYEA MGREQMMEMH
PMLRGFFGGE
//
