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Database: UniProt
Entry: A0A2U2J3Z4_9SPHN
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ID   A0A2U2J3Z4_9SPHN        Unreviewed;       453 AA.
AC   A0A2U2J3Z4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=DF286_09370 {ECO:0000313|EMBL:PWG03055.1};
OS   Sphingosinicella humi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingosinicellaceae; Sphingosinicella.
OX   NCBI_TaxID=2068657 {ECO:0000313|EMBL:PWG03055.1, ECO:0000313|Proteomes:UP000245916};
RN   [1] {ECO:0000313|EMBL:PWG03055.1, ECO:0000313|Proteomes:UP000245916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QZX222 {ECO:0000313|EMBL:PWG03055.1,
RC   ECO:0000313|Proteomes:UP000245916};
RA   Qiao Z., Wang G.;
RT   "Genome of Sphingosinicella humi QZX222.";
RL   Submitted (MAY-2018) 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 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: 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:PWG03055.1}.
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DR   EMBL; QFFF01000001; PWG03055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2J3Z4; -.
DR   OrthoDB; 9809248at2; -.
DR   Proteomes; UP000245916; 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:UP000245916};
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        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        123..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        225..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        327..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   453 AA;  49198 MW;  5CDDB5CB3B1F588D CRC64;
     MASHAEQLIG NINLANFAKA TDLKKRLWFT LGALVIFRLL TFVPLPGIDP RALDQLFQTT
     QGGVLDLFNM FSGGGLERMS LIALGVMPYI TASIVMQMAT SMSPNLAALK KEGESGRKKI
     NQYTRYGTVF LCIIQGYFVA VGLESWGAGQ GGSAVIDPGW MFRLTAVVNL VGGTMFLMWL
     GEQVTSRGVG NGVSLIITAG IVAQIPTGVA QALEGSRTGS LSPLLVLGVL AFAAILVLFI
     CFMELGQRRV LIQYPKRQTM HSGMKAERSH LPLKVNTANV IPPIFASSLL LMPLTVAQFA
     GNRVQGESFW GDMLITVTTA LQHGAPLYMF LYGAGIAFFC FFYTAVVFNP EETADNLKRY
     GGFIPGIRPG KRTEEYLDYV LTRITVTGAA YLTLTCLIPE YLIARAGIPF YLGGTSLIIV
     VNVTMDTVTQ IQSHLIAHQY GDLIKKAKLK GSR
//
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