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Database: UniProt
Entry: C3K8T8_PSEFS
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Original site: C3K8T8_PSEFS 
ID   C3K8T8_PSEFS            Unreviewed;       134 AA.
AC   C3K8T8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 101.
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:CAY46660.1};
GN   OrderedLocusNames=PFLU_0383 {ECO:0000313|EMBL:CAY46660.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY46660.1};
RN   [1] {ECO:0000313|EMBL:CAY46660.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY46660.1};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2] {ECO:0000313|EMBL:CAI2794707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAI2794707.1};
RA   Fortmann-Grote C.;
RL   Submitted (OCT-2023) 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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00237}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00237}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the TatB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00237}.
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DR   EMBL; OV986001; CAI2794707.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY46660.1; -; Genomic_DNA.
DR   RefSeq; WP_012721794.1; NC_012660.1.
DR   AlphaFoldDB; C3K8T8; -.
DR   PATRIC; fig|216595.4.peg.618; -.
DR   eggNOG; COG1826; Bacteria.
DR   HOGENOM; CLU_086034_1_1_6; -.
DR   OrthoDB; 9816005at2; -.
DR   Proteomes; UP001152918; Chromosome.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00237};
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};
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          82..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   134 AA;  14363 MW;  84E0C319449567D2 CRC64;
     MFGISFSELL LVGLVALLVL GPERLPGAAR TAGLWIGRLK RSFNAIKQEV EREIGADEIR
     RQLHNEHILS LEQEARKILS PVQEPAKPVE PVADNTIAPT VEAAPVQPTA PTEPAPTPAA
     SPAPHDPTLP PRAP
//
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