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Database: UniProt
Entry: A0A1M6GXI0_9RHOB
LinkDB: A0A1M6GXI0_9RHOB
Original site: A0A1M6GXI0_9RHOB 
ID   A0A1M6GXI0_9RHOB        Unreviewed;       192 AA.
AC   A0A1M6GXI0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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=SAMN05444417_2982 {ECO:0000313|EMBL:SHJ14610.1};
OS   Wenxinia saemankumensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHJ14610.1, ECO:0000313|Proteomes:UP000184292};
RN   [1] {ECO:0000313|EMBL:SHJ14610.1, ECO:0000313|Proteomes:UP000184292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100565 {ECO:0000313|EMBL:SHJ14610.1,
RC   ECO:0000313|Proteomes:UP000184292};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQYO01000005; SHJ14610.1; -; Genomic_DNA.
DR   RefSeq; WP_073332591.1; NZ_FQYO01000005.1.
DR   AlphaFoldDB; A0A1M6GXI0; -.
DR   STRING; 1447782.SAMN05444417_2982; -.
DR   OrthoDB; 7206969at2; -.
DR   Proteomes; UP000184292; 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.
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:UP000184292};
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          77..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   192 AA;  19888 MW;  C130ABF9F98C7556 CRC64;
     MFGLGWSETL LIAIVALIVV GPKDLPGLFR QVGQFTGKAR AMAREFSRAM EAAADEAGVK
     EVEKTLRAAA NPKSFGTDAV KNAMTDSGKR NVKPGGATQA LSKERAEARD RMAEGAARKA
     EERRAREAAE AEASDAAEMS DEPEPDFGSR PGATPAAAPM ADPAPARTTA PQPDPGAPAG
     TGQAAPQTET QS
//
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