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Database: UniProt
Entry: A0A2R4X2B8_9EURY
LinkDB: A0A2R4X2B8_9EURY
Original site: A0A2R4X2B8_9EURY 
ID   A0A2R4X2B8_9EURY        Unreviewed;       503 AA.
AC   A0A2R4X2B8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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   ECO:0000313|EMBL:AWB27925.1};
GN   ORFNames=HARCEL1_09470 {ECO:0000313|EMBL:AWB27925.1};
OS   Halococcoides cellulosivorans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halococcoides.
OX   NCBI_TaxID=1679096 {ECO:0000313|EMBL:AWB27925.1, ECO:0000313|Proteomes:UP000244727};
RN   [1] {ECO:0000313|EMBL:AWB27925.1, ECO:0000313|Proteomes:UP000244727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HArcel1 {ECO:0000313|EMBL:AWB27925.1,
RC   ECO:0000313|Proteomes:UP000244727};
RA   Sorokin D.Y., Toshchakov S.V., Samarov N.I., Korzhenkov A., Kublanov I.V.;
RT   "Halococcoides cellulosivorans gen. nov., sp. nov., an extremely halophilic
RT   cellulose-utilizing haloarchaeon from hypersaline lakes.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CP028858; AWB27925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R4X2B8; -.
DR   KEGG; harc:HARCEL1_09470; -.
DR   Proteomes; UP000244727; 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   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:UP000244727};
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        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        69..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        378..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   DOMAIN          38..73
FT                   /note="Translocon Sec61/SecY plug"
FT                   /evidence="ECO:0000259|Pfam:PF10559"
SQ   SEQUENCE   503 AA;  55077 MW;  5D70E1CA023ECC10 CRC64;
     MSWKDTAEPV LTRMPTVRRP QRHVPFKRKL MWTAGILVLY FFLTNVHLFG MPVDPEAGDA
     FGRFRSILAG GAGTIMHLGI GPIVTASIVL QLLGGADLLG LDTENNPRDQ VLYQGLQKFL
     VLVMICLTGL PMVFASDYLP ASRAVQELLP IGKMGLKWLI FAQIALGGVL ILYMDEIVSK
     WGVGSGVGLF IIAGVSQQLF GGLTIRQFGD AGSFADLSLG LIPRWAGFVS NWLNLGVGEV
     EFPTTVSGWL LTDAGLEIIP IITTILIFVI VVYAESVRVE IPLSHARVKG ARGRFPVKLI
     YASVLPMILV RALQANIQFL GQILHQQWAG MPGWVGQYAD EGAQVTGGVF YYLAPVQSRQ
     EWMWWLGGQA SNMEPWQIFL RVGIDLGIMV FAGGLFAIFW VETTGMGPES TAQQIQNSGM
     QIPGFRQNPS VLEKVLERYI PQVTVIGGML VGFLAVMANL LGTIGGVSGT GLLLTVSITY
     KIYEEIAEEQ LMEMHPMMRQ MFG
//
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