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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//