ID   SECY_PARDE              Reviewed;         182 AA.
AC   P72179;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Protein translocase subunit SecY;
DE   Flags: Fragment;
GN   Name=secY;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627;
RX   PubMed=9862211; DOI=10.1093/protein/11.10.917;
RA   Perrier V., Burlacu-Miron S., Boussac A., Meier A., Gilles A.M.;
RT   "Metal chelating properties of adenylate kinase from Paracoccus
RT   denitrificans.";
RL   Protein Eng. 11:917-923(1998).
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 (By
CC       similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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; U64202; AAB06327.1; -; Genomic_DNA.
DR   AlphaFoldDB; P72179; -.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3370.10; -; 1.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR023201; SecY_dom_sf.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF00344; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           <1..182
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131737"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          163..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   182 AA;  19854 MW;  FC7B445BF994C5F0 CRC64;
     IFASSLLLLP VTISTFSGNQ TGPIMSTVLA YFGPGQPLYL LFFAAMIVFF TYFYTYNVSF
     KTEDVAENLK NQGGFIPGIR PGKRTEDYLT YVVTRVLVIG SAYLAFVCLL PAARDHPRPA
     GDPLLLGGTS VLIVVSVVMD TINQVQSHLL AHQYEGLIEK SQLPGKRGKT GAAKPRKAPA
     RR