(data stored in ACNUC7421 zone)

SWISSPROT: Q5LW37_RUEPO

ID   Q5LW37_RUEPO            Unreviewed;       455 AA.
AC   Q5LW37;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN   Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN   ECO:0000313|EMBL:AAV93823.1};
GN   OrderedLocusNames=SPO0506 {ECO:0000313|EMBL:AAV93823.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93823.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93823.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93823.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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
CC       two domains form a lateral gate at the front which open onto the
CC       bilayer between TMs 2 and 7, and are clamped together by SecE at
CC       the back. The channel is closed by both a pore ring composed of
CC       hydrophobic SecY resides and a short helix (helix 2A) on the
CC       extracellular side of the membrane which forms a plug. The plug
CC       probably moves laterally to allow the channel to open. The ring
CC       and the pore may move independently. {ECO:0000256|HAMAP-
CC       Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC   -!- SUBUNIT: Component of the Sec protein translocase complex.
CC       Heterotrimer consisting of SecY, SecE and SecG subunits. The
CC       heterotrimers can form oligomers, although 1 heterotrimer is
CC       thought to be able to translocate proteins. Interacts with the
CC       ribosome. Interacts with SecDF, and other proteins may be
CC       involved. Interacts with SecA. {ECO:0000256|HAMAP-Rule:MF_01465}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01465}. Membrane {ECO:0000256|RuleBase:RU003484}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU003484}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC       {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU004349}.
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; CP000031; AAV93823.1; -; Genomic_DNA.
DR   RefSeq; WP_011046265.1; NC_003911.12.
DR   STRING; 246200.SPO0506; -.
DR   EnsemblBacteria; AAV93823; AAV93823; SPO0506.
DR   KEGG; sil:SPO0506; -.
DR   eggNOG; ENOG4105CGG; Bacteria.
DR   eggNOG; COG0201; LUCA.
DR   HOGENOM; HOG000080585; -.
DR   KO; K03076; -.
DR   OMA; QTYVISQ; -.
DR   OrthoDB; 1567535at2; -.
DR   BioCyc; RPOM246200:G1G48-513-MONOMER; -.
DR   Proteomes; UP000001023; 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;
DR   PRODOM; Q5LW37.
DR   SWISS-2DPAGE; Q5LW37.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484}.
FT   TRANSMEM     27     48       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM     79    103       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    123    143       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    155    174       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    186    208       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    214    236       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    274    296       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    316    338       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    370    392       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    398    418       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   COILED      106    126       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   455 AA;  49283 MW;  DAD4836EF20F14FD CRC64;
     MVSAAEQMAA NTSWSALGKA TDLRNRILFT LGLLIVYRLG TFIPVPGIDG VALREFMEQA
     GQGIGGMVSM FTGGALGRMG IFALGIMPYI SASIIVQLLT AMVPSLEQLK KEGEQGRKKI
     NQYTRLGTVA LATVQAYGLA VSLESGDLAT EPGMYFRFAT MITLVGGTMF LMWLGEQITA
     RGIGNGVSLI IFVGIIAEVP AALAQFFASG RSGAISPAVI IAIILMVIAV ITFVVFMERA
     LRKIHIQYPR RQVGMKVYDG GSSHLPVKVN PAGVIPAIFA SSLLLLPVTI STFSSGAANG
     PVMSWLLANF GPGQPLYLLF FVSMIVFFAY FYTFNVSFKP DDVAQNLKNQ NGFVPGIRPG
     KKTAEYLEYV VNRVLVLGSA YLAAVCLLPE IMRGQFNVPF YFGGTSVLII VSVTMDTIQQ
     VQSHLLAHQY EGLIEKSQLR GKNRKRTNRK GPARR
//

If you have problems or comments...

PBIL Back to PBIL home page