(data stored in SCRATCH zone)

SWISSPROT: Q3ILQ6_PSEHT

ID   Q3ILQ6_PSEHT            Unreviewed;       125 AA.
AC   Q3ILQ6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000256|HAMAP-Rule:MF_00422,
GN   ECO:0000313|EMBL:CAI85319.1};
GN   OrderedLocusNames=PSHAa0216 {ECO:0000313|EMBL:CAI85319.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85319.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85319.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Essential subunit of the Sec protein translocation
CC       channel SecYEG. Clamps together the 2 halves of SecY. May contact
CC       the channel plug during translocation. {ECO:0000256|HAMAP-
CC       Rule:MF_00422}.
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_00422}.
CC   -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family.
CC       {ECO:0000256|HAMAP-Rule:MF_00422, ECO:0000256|SAAS:SAAS00569815}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00422}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR954246; CAI85319.1; -; Genomic_DNA.
DR   RefSeq; WP_011326934.1; NC_007481.1.
DR   STRING; 326442.PSHAa0216; -.
DR   EnsemblBacteria; CAI85319; CAI85319; PSHAa0216.
DR   KEGG; pha:PSHAa0216; -.
DR   PATRIC; fig|326442.8.peg.207; -.
DR   eggNOG; ENOG4105PM1; Bacteria.
DR   eggNOG; COG0690; LUCA.
DR   HOGENOM; HOG000219148; -.
DR   KO; K03073; -.
DR   OMA; FLWLTDK; -.
DR   OrthoDB; POG091H04S8; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009306; P:protein secretion; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00422; SecE; 1.
DR   InterPro; IPR022943; SecE.
DR   InterPro; IPR005807; SecE_bac.
DR   InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR   Pfam; PF00584; SecE; 1.
DR   PRINTS; PR01650; SECETRNLCASE.
DR   TIGRFAMs; TIGR00964; secE_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILQ6.
DR   SWISS-2DPAGE; Q3ILQ6.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00422};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00422};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00084204};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00458895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00084172};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00084198};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00458914};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00422,
KW   ECO:0000256|SAAS:SAAS00084174}.
FT   TRANSMEM     17     34       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00422}.
FT   TRANSMEM     40     57       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00422}.
FT   TRANSMEM     88    109       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00422}.
SQ   SEQUENCE   125 AA;  13361 MW;  9B71876A16EBA6C2 CRC64;
     MSTNVETPSS AMESVKWLVA IVLLAGAVVG NHMFADQSVL LRAIGVVVAI AAGLAIASQT
     AKGRTFLTFA KEARIEVRKV IWPTRQETIH TTLIVMVATA IMALILWGLD GILFRAVGFL
     TGLEI
//

If you have problems or comments...

PBIL Back to PBIL home page