SECY_METTH
ID SECY_METTH Reviewed; 456 AA.
AC O26134;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=MTH_26;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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:0000255|HAMAP-Rule:MF_01465}.
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:0000255|HAMAP-Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; AE000666; AAB84535.1; -; Genomic_DNA.
DR PIR; F69132; F69132.
DR AlphaFoldDB; O26134; -.
DR SMR; O26134; -.
DR STRING; 187420.MTH_26; -.
DR EnsemblBacteria; AAB84535; AAB84535; MTH_26.
DR KEGG; mth:MTH_26; -.
DR PATRIC; fig|187420.15.peg.26; -.
DR HOGENOM; CLU_031763_3_0_2; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131765"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 22..48
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 49..59
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..88
FT /note="Discontinuously helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT INTRAMEM 60..67
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000250"
FT INTRAMEM 68..79
FT /evidence="ECO:0000250"
FT INTRAMEM 80..88
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..134
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 135..141
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..166
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 167..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..191
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 192..224
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 225..246
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 247..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 276..297
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 298..334
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 335..354
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 355..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 398..416
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 417..419
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 420..434
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 49790 MW; 134C8FBF97251859 CRC64;
MEQLKEKFEP LFSVLPQVKS PGYRVPFREK LKWTGIILVL YFFLAQIPLY GLSANAVDQF
AQFRAVLAGN FGSILTLGIG PIVSASIILQ LLVGGKILKL DLSRHEDKAF FQGLQKLLAI
VFTFFEALIF VLTGSLAPSA PQFVWVLILQ LTIGGILIIF LDEVVSKWGF GSGVGLFIAA
GVSQEIIVGA FNPLSAPTQP GVPAGRITGF LYLLFTGQSP DFQYYVLPVL ALIAVFLVVV
YAESMRVEIP ISMGGGKRLS RGAVGKYPLR FIYASNMPVI LTSALLLNVQ LLANVFQKLG
YPILGTVSNG QAVDGLAYLL TAPRSIDALI LDPFRVVFYA VVFIGLCVLF AWLWVEISNI
GPRHVARQLY QMGMQIPGFR SSRGQFEKIL KRYIPTITIL GGAFVGLLAF VADLTGSLGG
GTGVLLTVGI VYRLYEEIAQ EQLMDMHPIL RSFLGD
