ID A0A165ZLV5_9EURY Unreviewed; 454 AA.
AC A0A165ZLV5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:KZX10882.1};
GN ORFNames=MBORA_17190 {ECO:0000313|EMBL:KZX10882.1};
OS Methanobrevibacter oralis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX10882.1, ECO:0000313|Proteomes:UP000077428};
RN [1] {ECO:0000313|EMBL:KZX10882.1, ECO:0000313|Proteomes:UP000077428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX10882.1,
RC ECO:0000313|Proteomes:UP000077428};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL Submitted (APR-2016) 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 -!- 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:KZX10882.1}.
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DR EMBL; LWMU01000103; KZX10882.1; -; Genomic_DNA.
DR RefSeq; WP_042694566.1; NZ_LWMU01000103.1.
DR AlphaFoldDB; A0A165ZLV5; -.
DR STRING; 66851.MBORA_17190; -.
DR PATRIC; fig|66851.6.peg.1873; -.
DR OrthoDB; 371914at2157; -.
DR Proteomes; UP000077428; Unassembled WGS sequence.
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};
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 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 72..96
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 333..352
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT DOMAIN 38..71
FT /note="Translocon Sec61/SecY plug"
FT /evidence="ECO:0000259|Pfam:PF10559"
SQ SEQUENCE 454 AA; 49149 MW; 58390F15BEC9B76A CRC64;
MSSLEVLEPI FRLIPEVKAP VHTEEFNEKL KWTAIVLVLY FILTQIPLYG LAPGAVDQFA
QLRAVMAGNF GSILTLGIGP IVTASIVLQL LVGSNLLDLD LSSHKDKSHF QATQKVLSIV
FTVFEAGVLV LTGNLMPIDN SYMLVLLVQL VIGALVIIYL DEVVSKWGFG SGIGLFIAAG
VCQAIIVGTF NFFPTADGTL PGIIPGLIQA SMAGTPDFSV LIPLFATIIV FLIVLYGEAM
RVEIPISQGS VRGHGRVRGA VGKYPLKFVY ASNMPVILTS ALLVNVTLLS NVFQKIGYPI
LGRVENGKAV DGIAWLLSTP NNLSMFYTEP LHVLVYALFF LICCIIFSYL WVEISGLNAK
KISEQLYKSG IQIPGFRSSK RQLFKILKKY IPALTIISGI YVGLIAFLAD LTGALGGGTG
VLLTVGIIHK LYEEMAEEQL MSSNPLIRKV LGGD
//
