SECY_STACT
ID SECY_STACT Reviewed; 430 AA.
AC Q05217; B9DM43;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=Sca_1715;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=1435726; DOI=10.1007/bf00286192;
RA Tschauder S., Driessen A.J.M., Freudl R.;
RT "Cloning and molecular characterization of the secY genes from Bacillus
RT licheniformis and Staphylococcus carnosus: comparative analysis of nine
RT members of the SecY family.";
RL Mol. Gen. Genet. 235:147-152(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; X70086; CAA49691.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL28621.1; -; Genomic_DNA.
DR PIR; S30115; S30115.
DR RefSeq; WP_015900959.1; NC_012121.1.
DR AlphaFoldDB; Q05217; -.
DR SMR; Q05217; -.
DR STRING; 396513.SCA_1715; -.
DR GeneID; 60544566; -.
DR KEGG; sca:SCA_1715; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_9; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR BioCyc; SCAR396513:SCA_RS08740-MON; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..430
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131747"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 179..199
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 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT CONFLICT 5
FT /note="F -> I (in Ref. 1; CAA49691)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="T -> S (in Ref. 1; CAA49691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47386 MW; F50ED1310971FB95 CRC64;
MFETFVNFFK TKEVRNKIFF TLAMLVIFKI GTYIPAPGVN PAAFDNNQGS QGVTDLLNTF
GGGALKNFSI FAMGIMPYIT ASIVMQLLQM DIVPKFTEWA KQGDVGRKKL NNVTRYFAII
LAFIQSIGMA FQFNNYLKGA LIIDPSPMSY LLIAIVLTTG TAFLLWLGEQ ITQYGVGNGI
SIIIFAGILS TLPSSLIQFY QQAFVGQSDT TMAWLQVAGL VIGLVLLTMG AVYVLQAVRK
IPIQYAKKQS TQRLGSNATY LPLKVNSAGV IPVIFAMAFF LLPRTLTMFF PKADWAQQIA
NTANPSSNIG MVIYIILIIA FTYFYAFVQV NPEKMSDNLK KQGSYVPGIR PGEQTKKYIT
KVLYRLTFVG SIFLAVIAIL PILATKFMNL PQSIQVGGTS LLIVIGVAIE TMKSLEAQVN
QKEYKGFGGR
