ID A0A365P098_9FLAO Unreviewed; 448 AA.
AC A0A365P098;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=DPN68_09455 {ECO:0000313|EMBL:RBA27907.1};
OS Flavobacterium tibetense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2233533 {ECO:0000313|EMBL:RBA27907.1, ECO:0000313|Proteomes:UP000253319};
RN [1] {ECO:0000313|EMBL:RBA27907.1, ECO:0000313|Proteomes:UP000253319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH5 {ECO:0000313|EMBL:RBA27907.1,
RC ECO:0000313|Proteomes:UP000253319};
RA Xing P., Phurbu D., Lu H.;
RT "Flavobacterium tibetense sp. nov., isolated from a wetland YonghuCo on
RT Tibetan Plateau.";
RL Submitted (JUN-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: 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:RBA27907.1}.
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DR EMBL; QLST01000011; RBA27907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365P098; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000253319; 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: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:UP000253319};
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..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 150..173
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 215..241
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 272..296
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 373..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 448 AA; 49052 MW; DDA1A2B7D59580F8 CRC64;
MKRFIDSFIN VWKIEELKNR ILLTLGLLLV YRFGAQVTLP GIDATKLSNL TDQTDGGIGW
LINVFTGGAF SQASVFALGI MPYISASIVV QLMGIAVPYL QKLQKDGESG RKKINQITRW
LTILITLVQG PGYIYNLYRT LPTDAFLLGV SSFSFLFSSV LILVTGTIFA MWLGEKITDK
GIGNGISLLI MVGIIASMPQ AFIQEFLSRT TQANGSYMMI VIELILWFLV IIACILLVMA
VRKIPVQYAR RTASGDFEQD MMGSRQFIPL KLNASGVMPI IFAQAIMFIP AAVSGLAKES
DTAQSLAGMF NNPFGLVYNI VFALLIIIFT YFYTAITVPT NKMADDLKRS GGFIPGIRPG
VETGDYLDKV MSLITFPGSV FLALIAVLPA VVVSLLNVQG AWGYFYGGTS LLIMVGVAID
TIQQINSYLL NKHYDGLMKS GKNRKAVA
//
