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Database: UniProt
Entry: A0A1E5P6H1_9ACTN
LinkDB: A0A1E5P6H1_9ACTN
Original site: A0A1E5P6H1_9ACTN 
ID   A0A1E5P6H1_9ACTN        Unreviewed;       162 AA.
AC   A0A1E5P6H1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-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=AS594_12365 {ECO:0000313|EMBL:OEJ25158.1};
OS   Streptomyces agglomeratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ25158.1, ECO:0000313|Proteomes:UP000095759};
RN   [1] {ECO:0000313|EMBL:OEJ25158.1, ECO:0000313|Proteomes:UP000095759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ25158.1,
RC   ECO:0000313|Proteomes:UP000095759};
RA   Chen X.;
RT   "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT   novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL   Submitted (AUG-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}.
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:OEJ25158.1}.
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DR   EMBL; MEHJ01000001; OEJ25158.1; -; Genomic_DNA.
DR   RefSeq; WP_069927081.1; NZ_MEHN01000001.1.
DR   AlphaFoldDB; A0A1E5P6H1; -.
DR   STRING; 285458.BGM19_24445; -.
DR   OrthoDB; 3267321at2; -.
DR   Proteomes; UP000095759; 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:UP000095759};
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          105..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   162 AA;  17551 MW;  E218C17256ADCE17 CRC64;
     MFSDIGGLEL VTLVVLAVLV FGPEKLPKLI QDASAMIRKL REFSESAKQD IRSELGPEFK
     DFDFEDLNPK TFVRKQLMDN DDLGLKEIRS SFDLKSEMAE VADVVKGRDS GTPSGAVSGT
     NGSNGSAGKA NLTKDSTGTP DLLKKRETPA QSERPPFDAD AT
//
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