TATB_MYCGI
ID TATB_MYCGI Reviewed; 141 AA.
AC A4T8W2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; OrderedLocusNames=Mflv_2203;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_00237}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00237};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00237}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; CP000656; ABP44681.1; -; Genomic_DNA.
DR RefSeq; WP_011893089.1; NC_009338.1.
DR AlphaFoldDB; A4T8W2; -.
DR SMR; A4T8W2; -.
DR STRING; 350054.Mflv_2203; -.
DR EnsemblBacteria; ABP44681; ABP44681; Mflv_2203.
DR KEGG; mgi:Mflv_2203; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_2_0_11; -.
DR OMA; PRAVITK; -.
DR OrthoDB; 2073616at2; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00237; TatB; 1.
DR InterPro; IPR018448; TatB.
DR TIGRFAMs; TIGR01410; tatB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..141
FT /note="Sec-independent protein translocase protein TatB"
FT /id="PRO_1000078324"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT REGION 92..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 14771 MW; 7B2F36327888C874 CRC64;
MFANVGWGEM LVLVIAGLVI LGPERLPGAI RWTAGAVRQA RDYITGATSQ LREDLGPEFD
DLREPLSELQ KLRGMTPRAA LTKHLLDGDD SIFTGRFDST SSDQPGSGKP PKPQSGPGPA
AASGPAATTT PASTPFDPDA T
