ID A0A1I3XW18_9PSEU Unreviewed; 132 AA.
AC A0A1I3XW18;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05421835_11645 {ECO:0000313|EMBL:SFK23186.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFK23186.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFK23186.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFK23186.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the TatB family. {ECO:0000256|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; FORP01000016; SFK23186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3XW18; -.
DR STRING; 115433.SAMN05421835_11645; -.
DR OrthoDB; 3267321at2; -.
DR Proteomes; UP000199025; 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 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:UP000199025};
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 83..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 14500 MW; 7AFF80B68592A15C CRC64;
MFESVGWGEI LVLIVAGLFI LGPERLPEAA SWLAKGVRKV REFATGARQQ LRDEMGPEFE
EFRKPLEDLR QLRNFDPRRA ITNHLFDGDP DPLGLNGMSG GSTKPNGYPA VSGKAEESLK
PGEKPPVDPD AT
//
