ID A0A1H4Y687_9ACTN Unreviewed; 145 AA.
AC A0A1H4Y687;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN05216482_6116 {ECO:0000313|EMBL:SED13413.1};
OS Streptomyces sp. PAN_FS17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855351 {ECO:0000313|EMBL:SED13413.1, ECO:0000313|Proteomes:UP000199275};
RN [1] {ECO:0000313|Proteomes:UP000199275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA Varghese N., Submissions S.;
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; FNTN01000001; SED13413.1; -; Genomic_DNA.
DR RefSeq; WP_030946734.1; NZ_FNTN01000001.1.
DR AlphaFoldDB; A0A1H4Y687; -.
DR STRING; 1855351.SAMN05216482_6116; -.
DR OrthoDB; 3267321at2; -.
DR Proteomes; UP000199275; 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 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:UP000199275};
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 99..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 145 AA; 16332 MW; 9858C659AE7DB9DB CRC64;
MFNDIGPLEL VTLIVLAVLV FGPDKLPKLI QDVTRTIRKI REFSESAKED IRQELGPEFK
DFEFEDLNPK TFIRKQLDND ELGLKEIRNG FDLKKEMAEV TDAVHSRESE SSSSSSSGSS
GGSIDMTKKP ENPRDERPPY DADAT
//
