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Database: UniProt
Entry: A0A119CYF9_THIDE
LinkDB: A0A119CYF9_THIDE
Original site: A0A119CYF9_THIDE 
ID   A0A119CYF9_THIDE        Unreviewed;       437 AA.
AC   A0A119CYF9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000256|ARBA:ARBA00039733, ECO:0000256|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN   ECO:0000313|EMBL:KVW99723.1};
GN   ORFNames=ABW22_00755 {ECO:0000313|EMBL:KVW99723.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW99723.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW99723.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW99723.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
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 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:0000256|HAMAP-
CC       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: 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:KVW99723.1}.
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DR   EMBL; LDUG01000002; KVW99723.1; -; Genomic_DNA.
DR   RefSeq; WP_059750926.1; NZ_LDUG01000002.1.
DR   AlphaFoldDB; A0A119CYF9; -.
DR   STRING; 1123392.GCA_000376425_03447; -.
DR   PATRIC; fig|36861.3.peg.1187; -.
DR   eggNOG; COG0201; Bacteria.
DR   OrthoDB; 9809248at2; -.
DR   Proteomes; UP000064243; 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   GO; GO:0043952; P:protein transport by the Sec complex; 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   NCBIfam; TIGR00967; 3a0501s007; 1.
DR   PANTHER; PTHR10906:SF2; PREPROTEIN TRANSLOCASE SUBUNIT SCY2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 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|HAMAP-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:UP000064243};
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        18..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        70..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        178..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        207..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        266..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        391..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   437 AA;  47313 MW;  F225622FB6EC24FD CRC64;
     MATPKSGLNK FGDLKRRLLF LLGALIVYRI GTFIPVPGID PLVLDQLFKS QQGGILGMFN
     MFSGGALSRF SLFALGIMPY ISASIIVQLM TTVSPQLEAL KKEGESGRRK ITQYTRYGTL
     FLAVFQALGI SIALESQAGL VLDPGMGFRL ITVATLTAGT MFLMWLGEQI TERGLGNGIS
     IIIFAGIVAG LPSAIGGTLE LTRTGAFPIP LVLMLFVGVL LVTALVVFVE RGQRKILVNY
     AKRQVGKMVV GGQSSHLPLK LNMAGVIPPI FASSIILFPA TLAGWFGSGE GMGWLREIGS
     SLSPGQPVYV LAYALAIIFF CFFYTALVFN PKETADNLKK SGAFVPGIRP GDQTARYIDK
     ILTRLTLVGA IYITLVCLLP EFLILKWNVP FYFGGTSLLI IVVVTMDFMA QVQAYVMSHQ
     YEGLLKKANF KNGLAGR
//
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