ID A0A157S7L8_9BORD Unreviewed; 222 AA.
AC A0A157S7L8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ECO:0000313|EMBL:SAI66407.1};
GN ORFNames=SAMEA3906486_00946 {ECO:0000313|EMBL:SAI66407.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI66407.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI66407.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI66407.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-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; FKIF01000002; SAI66407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A157S7L8; -.
DR STRING; 288768.SAMEA3906486_00946; -.
DR OrthoDB; 9816005at2; -.
DR Proteomes; UP000076848; Unassembled WGS sequence.
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.
DR SUPFAM; SSF47162; Apolipoprotein; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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:UP000076848};
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 118..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 222 AA; 22750 MW; 81ED89474EC3482B CRC64;
MFDVSFTELL IIGVVALVVI GPERLPKVAR TVGHLLGRAQ RYVNDVKSDI QREIELDELR
KFKENMDAAA SDMQNTLRDT ENSLRSAEQS IRADLGTTSQ EVKEAAAATL QEAKASVSSA
AQEVKEALDS DKPANEPATE PAPSPSGAAA PAAEAVITAA APGSTPAATP VQTAAAASVA
APVPAPVAPA PIAPHDGQAV RPPPTPAPEP APKNPPPTGT PT
//