ID Q9PE56_XYLFA Unreviewed; 457 AA.
AC Q9PE56;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN OrderedLocusNames=XF_1172 {ECO:0000313|EMBL:AAF83982.1};
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF83982.1, ECO:0000313|Proteomes:UP000000812};
RN [1] {ECO:0000313|EMBL:AAF83982.1, ECO:0000313|Proteomes:UP000000812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c {ECO:0000313|EMBL:AAF83982.1,
RC ECO:0000313|Proteomes:UP000000812};
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.,
RA Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C., Lemos E.G., Lemos M.V., Lopes S.A.,
RA Lopes C.R., Machado J.A., Machado M.A., Madeira A.M., Madeira H.M.,
RA Marino C.L., Marques M.V., Martins E.A., Martins E.M., Matsukuma A.Y.,
RA Menck C.F., Miracca E.C., Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H.,
RA Nagai M.A., Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G.,
RA Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C.,
RA Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr.,
RA Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J.,
RA de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.,
RA da Silva A.M., da Silva F.R., da Silva W.A.Jr., da Silveira J.F.,
RA Silvestri M.L., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F.,
RA Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A.,
RA Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J.,
RA Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01465}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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; AE003849; AAF83982.1; -; Genomic_DNA.
DR PIR; E82714; E82714.
DR RefSeq; WP_010893685.1; NC_002488.3.
DR AlphaFoldDB; Q9PE56; -.
DR STRING; 160492.XF_1172; -.
DR KEGG; xfa:XF_1172; -.
DR PATRIC; fig|160492.11.peg.1239; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_2_6; -.
DR Proteomes; UP000000812; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01465};
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};
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..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 75..99
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 151..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 216..239
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 271..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 457 AA; 49119 MW; 7575DBB2BA9E6719 CRC64;
MSQPGLGNLG NRFGKSIELR HRLLFLFGAL IVYRVGCYVP VPGVNPEAML ALMQKQGGGI
VDMFNMFSGG ALHRFSIFAL NVMPYISASI VVQLATHIFP SLKAMQKEGE SGRRKITQYS
RIGAVILAVI QGGSIALALQ NQTAPGGAAV VYAPGAAFVM TAIVALTAGT VFLMWVGEQV
TERGIGNGVS MIIFAGIVAG LPGSVLQIID AFRSDALSLI SLLIIVFIVL SFTFFVVFVE
RGLRRITVNY ARRVEGRNSY MNKSSFLPLK LNMAGVIPPI FASSILAFPV TLSMWSGQAS
SNTVFGAWLQ RVSSALGPGE PLHMILFAVL IIGFAFFYTA LVFSSQETAD ILKKSGALIP
GIRPGKATSD YVDGVLTRLT AVGSLYLVIV CLLPEFMQSR MGASFHFGGT SLLIAVVVVM
DFISQIQVHQ ASNQYDGVGF LKKANLKGVS KRRRFVN
//
