TATA_SHESH
ID TATA_SHESH Reviewed; 78 AA.
AC A8G0T0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236};
GN Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; OrderedLocusNames=Ssed_4099;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC transports large folded proteins containing a characteristic twin-
CC arginine motif in their signal peptide across membranes. TatA could
CC form the protein-conducting channel of the Tat system.
CC {ECO:0000255|HAMAP-Rule:MF_00236}.
CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC complex, containing multiple copies of TatA, TatB and TatC subunits,
CC and a separate TatA complex, containing only TatA subunits. Substrates
CC initially bind to the TatABC complex, which probably triggers
CC association of the separate TatA complex to form the active translocon.
CC {ECO:0000255|HAMAP-Rule:MF_00236}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00236}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
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; CP000821; ABV38703.1; -; Genomic_DNA.
DR RefSeq; WP_012144433.1; NC_009831.1.
DR AlphaFoldDB; A8G0T0; -.
DR SMR; A8G0T0; -.
DR STRING; 425104.Ssed_4099; -.
DR EnsemblBacteria; ABV38703; ABV38703; Ssed_4099.
DR KEGG; sse:Ssed_4099; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_5_3_6; -.
DR OMA; HWIVILV; -.
DR OrthoDB; 1907955at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01411; tatAE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..78
FT /note="Sec-independent protein translocase protein TatA"
FT /id="PRO_1000078322"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 78 AA; 8413 MW; B7535375F02766B6 CRC64;
MGGISIWQLL IVALIVVLLF GTKKLRSLGG DLGGAVKGFK SAMSSEEEKK AIEDSASEKT
AQTEEKKTES KDKDKEQV