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Database: UniProt
Entry: U3U3N5_9ENTR
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Original site: U3U3N5_9ENTR 
ID   U3U3N5_9ENTR            Unreviewed;       443 AA.
AC   U3U3N5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN   Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN   ECO:0000313|EMBL:BAN98816.1};
GN   ORFNames=E05_40500 {ECO:0000313|EMBL:BAN98816.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN98816.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN98816.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
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}.
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DR   EMBL; AP012551; BAN98816.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3U3N5; -.
DR   KEGG; psts:E05_40500; -.
DR   eggNOG; COG0201; Bacteria.
DR   HOGENOM; CLU_030313_0_2_6; -.
DR   Proteomes; UP000016901; 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   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:SF9; PREPROTEIN TRANSLOCASE SUBUNIT SCY1, 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:UP000016901};
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        23..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        75..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        186..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        215..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        274..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        316..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        373..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        397..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   443 AA;  48734 MW;  3A02387BFE69FABD CRC64;
     MAKQPGLDFQ SAKGGFGELK RRLLFVIGAL IVFRIGSFIP IPGIDATVLV KLLEQQRGTI
     IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP ALAEIKKEGE AGRRKISQYT
     RYGTLVLAIF QSIGIATGLP NMPGMQGLVL NPDFAFYFTA VVSLVTGTMF LMWLGEQITE
     RGIGNGISII IFAGIVAGLP PAIGHTIEQA RQGDLHFLLL LLVAVLVFAV TFFVIFVERG
     QRRIVVNYAK RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI AFWFGGGTGW
     NWLTTISLYL QLGQPLYVLL YATAIIFFCF FYTALVFNPR ETADNLKKSG AFVPGIRPGE
     QTAKYIDKVM TRLTLIGALY ITFICLIPEF MRDAMKVPFY FGGTSLLIVV VVIMDFMAQV
     QTLMMSSQYE SALKKANLKG YGR
//
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