ID   TATA_BORPD              Reviewed;          75 AA.
AC   A9HWB1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236};
GN   Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; OrderedLocusNames=Bpet0129;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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. TatA could
CC       form the protein-conducting channel of the Tat system.
CC       {ECO:0000255|HAMAP-Rule:MF_00236}.
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_00236}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00236}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00236}.
CC   -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC       Rule:MF_00236}.
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DR   EMBL; AM902716; CAP40460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9HWB1; -.
DR   SMR; A9HWB1; -.
DR   STRING; 94624.Bpet0129; -.
DR   EnsemblBacteria; CAP40460; CAP40460; Bpet0129.
DR   KEGG; bpt:Bpet0129; -.
DR   eggNOG; COG1826; Bacteria.
DR   OMA; HWIVILV; -.
DR   Proteomes; UP000001225; Chromosome.
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_00236; TatA_E; 1.
DR   InterPro; IPR003369; TatA/B/E.
DR   InterPro; IPR006312; TatA/E.
DR   Pfam; PF02416; TatA_B_E; 1.
DR   TIGRFAMs; TIGR01411; tatAE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..75
FT                   /note="Sec-independent protein translocase protein TatA"
FT                   /id="PRO_1000125196"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT   REGION          44..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   75 AA;  8161 MW;  EAE0CCC1F2E0AE94 CRC64;
     MGSFSIWHWL IVLVIVALVF GTKKLRNIGS DLGGAVKGFK EGMKDANSDK PAEQVTQQKV
     ADDTIDVQAK EKTNS