TATB_SODGM
ID TATB_SODGM Reviewed; 232 AA.
AC Q2NWT7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; OrderedLocusNames=SG0113;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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}.
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; AP008232; BAE73388.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NWT7; -.
DR SMR; Q2NWT7; -.
DR STRING; 343509.SG0113; -.
DR EnsemblBacteria; BAE73388; BAE73388; SG0113.
DR KEGG; sgl:SG0113; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_1_0_6; -.
DR OMA; MFEVGWT; -.
DR BioCyc; SGLO343509:SGP1_RS26200-MON; -.
DR Proteomes; UP000001932; 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_00237; TatB; 1.
DR InterPro; IPR018448; TatB.
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..232
FT /note="Sec-independent protein translocase protein TatB"
FT /id="PRO_0000301243"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT REGION 108..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 232 AA; 23902 MW; 230265DDCF186140 CRC64;
MFDIGFGELM LLFVIGLVVL GPERLPVAVR TVTGWIRAIR SMASTVQNEL TQELKLQELQ
DSLKKVEEAS KNNLSPELKA SMEELREAAE SMKKYFKGIN SAALDPTEPH TIHNPLVTDP
EALHDGVTPA EGDRQAEAPL MAPSVKASAP ADSVANPGEP IAAAAIGQPA AASVDAASTS
PSAKVSAPAD SAANLATQAA TPAAPAPAPE EPGRAATATG PASSTSPLNN DR