ID L8XVN3_9GAMM Unreviewed; 473 AA.
AC L8XVN3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN ORFNames=F387_00813 {ECO:0000313|EMBL:ELV08083.1};
OS Wohlfahrtiimonas chitiniclastica SH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Wohlfahrtiimonas.
OX NCBI_TaxID=1261130 {ECO:0000313|EMBL:ELV08083.1, ECO:0000313|Proteomes:UP000011617};
RN [1] {ECO:0000313|EMBL:ELV08083.1, ECO:0000313|Proteomes:UP000011617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH04 {ECO:0000313|EMBL:ELV08083.1,
RC ECO:0000313|Proteomes:UP000011617};
RX PubMed=23558531;
RA Cao X.M., Chen T., Xu L.Z., Yao L.S., Qi J., Zhang X.L., Yan Q.L.,
RA Deng Y.H., Guo T.Y., Wang J., Hu K.X., Xu B.L.;
RT "Complete Genome Sequence of Wohlfahrtiimonas chitiniclastica Strain SH04,
RT Isolated from Chrysomya megacephala Collected from Pudong International
RT Airport in China.";
RL Genome Announc. 1:E0011913-E0011913(2013).
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}.
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:ELV08083.1}.
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DR EMBL; AOBV01000007; ELV08083.1; -; Genomic_DNA.
DR RefSeq; WP_008315906.1; NZ_KB372780.1.
DR AlphaFoldDB; L8XVN3; -.
DR GeneID; 58263927; -.
DR PATRIC; fig|1261130.3.peg.1233; -.
DR HOGENOM; CLU_030313_0_2_6; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000011617; 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.
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:UP000011617};
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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 340..359
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"
FT TRANSMEM 424..442
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 473 AA; 51605 MW; 7548023E75509602 CRC64;
MKNNQLPQFG NLSELKSRFI FLILALVVYR LGVHITVPGI NVPLLMDQMT QPGEGQGLSA
MMNLFSGGAF ERMSIFMLGV MPYITASIVI QMLTVVYPPL EQIKKEGQAG RRKITQYTRY
LTIVFAAAQG TAYAFGIVNG SLGFNSSIVV IPALNFVLLA VITWITGTIF LMWLGEQISE
RGIGNGISMI IFASILMGLP TGVSALFDTA RTEGGALAYL KVVFVILFVM AIVLLVVFIE
RGQRRITINY ARKQQGRQMS IGGQTTHLPL KLNMAGVIPA IFGSAFLSFV YTISAALAKI
EVSVAEGPVS GFAKFGYLAS QFFQKIGNYG VKYFTPGQPA YMILFAALII FFCFFYTAIQ
FNSKETAENL KRSGGFIPGI RPGIQTSQFF DKVLTRITLW GALYITAICL LPEMLGAIFN
FPSYFGGTSI LIAVVVVMDL IAQVQAQLVS QQYSSVMKKA NISSALNGKP PSI
//
