ID W8F954_9BACT Unreviewed; 438 AA.
AC W8F954;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN ORFNames=Hsw_3586 {ECO:0000313|EMBL:AHJ99181.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ99181.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ99181.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ99181.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) 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}.
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}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; CP007145; AHJ99181.1; -; Genomic_DNA.
DR RefSeq; WP_044003235.1; NZ_CP007145.1.
DR AlphaFoldDB; W8F954; -.
DR STRING; 1227739.Hsw_3586; -.
DR KEGG; hsw:Hsw_3586; -.
DR PATRIC; fig|1227739.3.peg.3743; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_10; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000019423; 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.
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:UP000019423};
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 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 72..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 438 AA; 47469 MW; C24C4C638B65CC87 CRC64;
MNKFITTIKN IFAIEDLRMR IFNTLFFIAI YRLGSYVVLP GVDPTRLKQG GATGVLGILD
TLLGGAFSHA SIFALGIMPY ISASIVLQLL TIAVPYFQKL QKEGESGRKK INQYTRVLTI
PIVALQSVGF IATINADAIL NPGVFFTIST AMIVTAGTLF CMWLGEKITD KGIGNGISMI
IMIGIVSRLP GALIGEAQAR TMRGSLVFLI ELVVLFLVVM AVIILTQAVR QIPVQYAKQI
GGAASLSSQR QYIPMKVNAA GVMPIIFAQS LMFVPAIAAS AWNKDSETAG LIGTWFQPNH
WVYNVVFGLL IIIFTYFYTA ISVNPNQIAD DLKRSGGFIP GVKPGRDTSE YIDEVLTRIT
LPGAVALAVI AILPSLATVA GVTRPFAQFF GGTSLIIMVG VVLDTMNQVK SYLLMRHYDG
MMKTGKERGR SRNIALAS
//
