SECY_MYCCT
ID SECY_MYCCT Reviewed; 482 AA.
AC P10250; Q2SRH2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=MCAP_0677;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3481422; DOI=10.1007/bf00325700;
RA Ohkubo S., Muto A., Kawauchi Y., Yamao F., Osawa S.;
RT "The ribosomal protein gene cluster of Mycoplasma capricolum.";
RL Mol. Gen. Genet. 210:314-322(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06414; CAA29723.1; -; Genomic_DNA.
DR EMBL; CP000123; ABC01495.1; -; Genomic_DNA.
DR PIR; S02850; BWYMSY.
DR RefSeq; WP_011387532.1; NC_007633.1.
DR AlphaFoldDB; P10250; -.
DR SMR; P10250; -.
DR TCDB; 3.A.5.3.1; the general secretory pathway (sec) family.
DR EnsemblBacteria; ABC01495; ABC01495; MCAP_0677.
DR GeneID; 23778369; -.
DR KEGG; mcp:MCAP_0677; -.
DR HOGENOM; CLU_030313_0_1_14; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR PhylomeDB; P10250; -.
DR Proteomes; UP000001928; 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..482
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131733"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 325
FT /note="A -> G (in Ref. 1; CAA29723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53315 MW; 02A1E6AA2DE28CBD CRC64;
MVIKKPANKV DKKSTFKSSN KKKNPFKSSF LTKNKDLIYR ILFTLLALII IRLGVYITVP
GVTLDKRFAT DSSRIQFFQL LSTLGGGSIG RFSILALGVS PYITASIIVQ LLSTDVIPVL
TRWSKSGERG RKKLDKLTKI IMIPFALMQA EATIFTLSSQ GLIIPGWDNT NAIANSAFYY
ILIPLVMLGG SFFMLWIADQ ITIKGIGNGI SIVIFIGIII SMPSNLKSTF EYWVSNSGEE
ANIFFSGLLN FMIYISVFLL VILSVVIMNE AERKIPIQQT GSGLTDSSEH TPYLPLKLNN
AGVIPVIFAS AIISTPITIS QIIEAVNPDS GFVIFTRDYL SFNTWWGISI FGILIVLFTF
LYSQVQINPE KIAENFQKSG TFIPGIKPGK DTTKYLTGII NRLSVVGSVF LAIIALLPYV
ISKLTQLPSN LAIGGTGLII CISVAIQTVQ QLKGRIIQQN FIEKKKEKFT NNINKNKTSH
IW
