SECY_VIBCH
ID SECY_VIBCH Reviewed; 444 AA.
AC P78283; Q9KP04;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=VC_2576;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX PubMed=9322765; DOI=10.1016/s0378-1119(97)00238-2;
RA Bhattacharyya D., Das J.;
RT "The secY gene of V. cholerae: identification, cloning and
RT characterization.";
RL Gene 196:261-266(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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:0000255|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:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; Y08367; CAA69654.1; -; Genomic_DNA.
DR EMBL; Y07817; CAA69151.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95717.1; -; Genomic_DNA.
DR PIR; B82057; B82057.
DR RefSeq; NP_232204.1; NC_002505.1.
DR RefSeq; WP_000101599.1; NZ_LT906614.1.
DR AlphaFoldDB; P78283; -.
DR SMR; P78283; -.
DR STRING; 243277.VC_2576; -.
DR PRIDE; P78283; -.
DR DNASU; 2615593; -.
DR EnsemblBacteria; AAF95717; AAF95717; VC_2576.
DR GeneID; 57741178; -.
DR KEGG; vch:VC_2576; -.
DR PATRIC; fig|243277.26.peg.2455; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_2_6; -.
DR OMA; FAMWLGE; -.
DR BioCyc; VCHO:VC2576-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; -; 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 PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131758"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT CONFLICT 17
FT /note="S -> R (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="I -> M (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Missing (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="P -> R (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..210
FT /note="Missing (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> L (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="A -> C (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..301
FT /note="ESSTF -> AHS (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="T -> S (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="I -> N (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="R -> P (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="F -> L (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..424
FT /note="VQTH -> GTTL (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> D (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="Y -> L (in Ref. 1; CAA69654/CAA69151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 48664 MW; 9608C4FDB9FC89CF CRC64;
MARKPGQDFR SAQSGLSELK SRLFFVIGAL LVFRAGSFVP IPGIDAAVLA ELFEQQKGTI
VEMFNMFSGG ALERASILAL GIMPYISASI VVQLLTVVHP ALAELKKEGE AGRRKISQYT
RYGTLVLATF QAIGIATGLP NMVNNLVVID QTMFTLIATV SLVTGTMFLM WLGEQITERG
IGNGISILIF AGIVAGLPKA IGQTIEQARQ GELHVLLLLL IAVLAFAVIY FVVFMERGQR
RIVVNYAKRQ QGRKVFAAQS THLPLKINMA GVIPAIFASS IILFPGTLAQ WFGQNGESST
FGWLTDVSLA LSPGQPLYVM LYAAAIIFFC FFYTALVFNP RETADNLKKS GAFVPGIRPG
EQTAKYIDKV MTRLTLAGAL YITFICLIPE FMMVAWNVRF YFGGTSLLIV VVVIMDFMAQ
VQTHLMSHQY ESVLKKANLK GYGR
