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Database: UniProt
Entry: A0A074TG72_9RHOB
LinkDB: A0A074TG72_9RHOB
Original site: A0A074TG72_9RHOB 
ID   A0A074TG72_9RHOB        Unreviewed;       213 AA.
AC   A0A074TG72;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=DL1_16240 {ECO:0000313|EMBL:KEP70649.1};
OS   Thioclava dalianensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP70649.1, ECO:0000313|Proteomes:UP000027725};
RN   [1] {ECO:0000313|EMBL:KEP70649.1, ECO:0000313|Proteomes:UP000027725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP70649.1,
RC   ECO:0000313|Proteomes:UP000027725};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL   Submitted (MAR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEP70649.1}.
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DR   EMBL; JHEH01000005; KEP70649.1; -; Genomic_DNA.
DR   RefSeq; WP_038063947.1; NZ_JHEH01000005.1.
DR   AlphaFoldDB; A0A074TG72; -.
DR   STRING; 1185766.SAMN05216224_102184; -.
DR   eggNOG; COG1826; Bacteria.
DR   OrthoDB; 7206969at2; -.
DR   Proteomes; UP000027725; 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:UP000027725};
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   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          91..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  21598 MW;  02BF06E885AD5E88 CRC64;
     MFDIGWSELL VIGVVALIVV GPKDLPKMFH QLGRFTAKAK SMAREFSSAM EDAAKDSGLD
     EAAGSVRDLK SLTSKKALGL DALERAADSF EKWDPKAPSA RSKTAGLVPD PEAAPPKPAS
     ALAETATESV AKDTAAPAAK PAAKTGTARK PAAAKKPAAK KPAAKAASKS TTGKTTAAKP
     AAAKTTAAKS ATAKKPAAKK AKAAKAAPKK DQA
//
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