SECY_ALKHC
ID SECY_ALKHC Reviewed; 430 AA.
AC P38375; Q9Z9J5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=BH0154;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=1512566; DOI=10.1099/00221287-138-7-1365;
RA Kang S.K., Kudo T., Horikoshi K.;
RT "Molecular cloning and characterization of an alkalophilic Bacillus sp.
RT C125 gene homologous to Bacillus subtilis secY.";
RL J. Gen. Microbiol. 138:1365-1370(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10192928; DOI=10.1271/bbb.63.452;
RA Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.;
RT "Sequence analysis of a 32-kb region including the major ribosomal protein
RT gene clusters from alkaliphilic Bacillus sp. strain C-125.";
RL Biosci. Biotechnol. Biochem. 63:452-455(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC proteins may be involved. Interacts with SecA. {ECO:0000255|HAMAP-
CC 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; D10360; BAA01191.1; -; Genomic_DNA.
DR EMBL; AB017508; BAA75291.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB03873.1; -; Genomic_DNA.
DR PIR; B44859; B44859.
DR PIR; T44403; T44403.
DR RefSeq; WP_010896337.1; NC_002570.2.
DR AlphaFoldDB; P38375; -.
DR SMR; P38375; -.
DR STRING; 272558.10172766; -.
DR EnsemblBacteria; BAB03873; BAB03873; BAB03873.
DR KEGG; bha:BH0154; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_9; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR Proteomes; UP000001258; 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 GO; GO:0043952; P:protein transport by the Sec complex; 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 PANTHER; PTHR10906; PTHR10906; 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..430
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131709"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT CONFLICT 119
FT /note="V -> VV (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="F -> L (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="P -> L (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="L -> R (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> A (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="R -> P (in Ref. 1; BAA01191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 46910 MW; BFBF237C0920B435 CRC64;
MFRTISNIFR VGDLRRKVIF TLLMLIVFRI GSFIPVPGTN REVLDFVDQA NAFGFLNTFG
GGALGNFSIF AMGIMPYITA SIVMQLLQMD VVPKFAEWAK EGEAGRRKLA QFTRYGTIVL
GFIQALGMSV GFNNFFPGLI PNPSVSVYLF IALVLTAGTA FLMWLGEQIT AKGVGNGISI
IIFAGIAAGI PNGLNLIYST RIQDAGEQLF LNIVVILLLA LAILAIIVGV IFVQQALRKI
PVQYAKRLVG RNPVGGQSTH LPLKVNAAGV IPVIFALSLF IFPPTVAGLF GSDHPVAAWV
IETFDYTHPI GMAVYALLII GFTYFYTFIQ VNPERMAENL KKQGGYIPGI RPGKATQTYI
TRILYRLTFV GSLFLAVVAI LPVFFIKFAD LPQAIQIGGT GLLIVVGVAL DTMKQIEAQL
IKRSYKGFIK
