TATB_SHESR
ID TATB_SHESR Reviewed; 147 AA.
AC Q0HZQ1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN OrderedLocusNames=Shewmr7_0401;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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. Together with
CC TatC, TatB is part of a receptor directly interacting with Tat signal
CC peptides. TatB may form an oligomeric binding site that transiently
CC accommodates folded Tat precursor proteins before their translocation.
CC {ECO:0000255|HAMAP-Rule:MF_00237}.
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_00237}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00237}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; CP000444; ABI41404.1; -; Genomic_DNA.
DR RefSeq; WP_011624284.1; NC_008322.1.
DR AlphaFoldDB; Q0HZQ1; -.
DR SMR; Q0HZQ1; -.
DR EnsemblBacteria; ABI41404; ABI41404; Shewmr7_0401.
DR KEGG; shm:Shewmr7_0401; -.
DR HOGENOM; CLU_086034_1_0_6; -.
DR OMA; GQFQEAM; -.
DR OrthoDB; 2073616at2; -.
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_00237; TatB; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR018448; TatB.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01410; tatB; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..147
FT /note="Sec-independent protein translocase protein TatB"
FT /id="PRO_0000301238"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT REGION 68..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 15944 MW; 306AE0A423E003A5 CRC64;
MFDGIGFMEL LLIGVLGLVV LGPERLPVAV RSVTGWIRAM KRMANSVKEE LEQELKIEQL
HADLKKAESK GLSNLSPELQ ESIDQLKQAA QSVNRPYQVQ DIPAQENQIH NPASQSVSSE
ASPTASSAPT SEPNQGEDTR SNPKANG
