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Database: UniProt
Entry: A0A1U9NED5_9GAMM
LinkDB: A0A1U9NED5_9GAMM
Original site: A0A1U9NED5_9GAMM 
ID   A0A1U9NED5_9GAMM        Unreviewed;       152 AA.
AC   A0A1U9NED5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, 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   ORFNames=B0D95_18205 {ECO:0000313|EMBL:AQT61814.1};
OS   Cellvibrio sp. PSBB023.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT61814.1, ECO:0000313|Proteomes:UP000189646};
RN   [1] {ECO:0000313|EMBL:AQT61814.1, ECO:0000313|Proteomes:UP000189646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB023 {ECO:0000313|EMBL:AQT61814.1,
RC   ECO:0000313|Proteomes:UP000189646};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; CP019799; AQT61814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9NED5; -.
DR   STRING; 1945512.B0D95_18205; -.
DR   KEGG; ceb:B0D95_18205; -.
DR   OrthoDB; 9816005at2; -.
DR   Proteomes; UP000189646; 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 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:UP000189646};
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          86..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   152 AA;  16866 MW;  6A75C0DB6F2AD105 CRC64;
     MFDIGFTELL VCLVVALVVI GPEQLPGTVR TVGLWIGRLK RSLRETRSEI ERQIGADDIR
     RQLHNEEILQ NIEETRRQFQ NVIDESANAI QPPALGVDNA DEQARRERSG QYGSPEELPD
     HAHTQDQQAP VTTEAAVTDK PVTPTPPTGT GH
//
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