ID A0A1H1QWG4_9PSED Unreviewed; 158 AA.
AC A0A1H1QWG4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000256|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000256|HAMAP-Rule:MF_00237};
GN ORFNames=SAMN05216598_1080 {ECO:0000313|EMBL:SDS27804.1};
OS Pseudomonas asplenii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=53407 {ECO:0000313|EMBL:SDS27804.1, ECO:0000313|Proteomes:UP000199524};
RN [1] {ECO:0000313|Proteomes:UP000199524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23835 {ECO:0000313|Proteomes:UP000199524};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00237}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00237};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00237}.
CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000256|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; LT629777; SDS27804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1QWG4; -.
DR Proteomes; UP000199524; Chromosome i.
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 Gene3D; 1.20.5.3310; -; 1.
DR HAMAP; MF_00237; TatB; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR018448; TatB.
DR NCBIfam; TIGR01410; tatB; 1.
DR PANTHER; PTHR33162; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR33162:SF1; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA, CHLOROPLASTIC; 1.
DR Pfam; PF02416; TatA_B_E; 1.
DR PRINTS; PR01506; TATBPROTEIN.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00237};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00237};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00237}; Reference proteome {ECO:0000313|Proteomes:UP000199524};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00237};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00237};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00237};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00237}.
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 16480 MW; 795E111BE94E1695 CRC64;
MFGISFSELL LVGLVALLVL GPERLPGAAR TAGLWVGRLK RSFNAIKQEV EREIGADEIR
RQLHNEHILS LEQEARKILS PVQEPVVQAQ PVAEAATAPA GAPLPSDLPP VTVAPGDAVP
VLGAVEPAPN LPTTTEAVPA PTPSAPASQD PTLPPRAP
//
