ID C6X8Q5_METGS Unreviewed; 72 AA. AC C6X8Q5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000256|HAMAP-Rule:MF_00236}; GN Name=tatA {ECO:0000256|HAMAP-Rule:MF_00236}; GN OrderedLocusNames=Msip34_0276 {ECO:0000313|EMBL:ACT49525.1}; OS Methylovorus glucosotrophus (strain SIP3-4). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49525.1, ECO:0000313|Proteomes:UP000002743}; RN [1] {ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACT49525.1, ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT49525.1, RC ECO:0000313|Proteomes:UP000002743}; RX PubMed=21622745; DOI=10.1128/JB.00404-11; RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A., RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S., RA Lidstrom M.E., Ivanova N., Chistoserdova L.; RT "Genomes of three methylotrophs from a single niche uncover genetic and RT metabolic divergence of Methylophilaceae."; RL J. Bacteriol. 193:3757-3764(2011). 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:0000256|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:0000256|HAMAP-Rule:MF_00236}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00236}; Single-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00236}. CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000256|HAMAP- CC Rule:MF_00236}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001674; ACT49525.1; -; Genomic_DNA. DR RefSeq; WP_013441104.1; NC_012969.1. DR AlphaFoldDB; C6X8Q5; -. DR STRING; 582744.Msip34_0276; -. DR KEGG; mei:Msip34_0276; -. DR eggNOG; COG1826; Bacteria. DR HOGENOM; CLU_086034_5_3_4; -. DR OrthoDB; 7066617at2; -. DR Proteomes; UP000002743; Chromosome. 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_00236; TatA_E; 1. DR InterPro; IPR003369; TatA/B/E. DR InterPro; IPR006312; TatA/E. DR NCBIfam; TIGR01411; tatAE; 1. DR PANTHER; PTHR42982; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1. DR PANTHER; PTHR42982:SF1; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1. DR Pfam; PF02416; TatA_B_E; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP- KW Rule:MF_00236}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00236}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00236}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP- KW Rule:MF_00236}; Reference proteome {ECO:0000313|Proteomes:UP000002743}; KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP- KW Rule:MF_00236}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00236}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00236}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00236}. FT TRANSMEM 6..22 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00236" FT REGION 44..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..72 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 72 AA; 7823 MW; 3F2833AC7C5BF626 CRC64; MGSFSIWHWL IVLVIVVLIF GTKKLRNMGS DVGGAVKNFK DAMNEGAQKP GSLDDRGTSN TVEGEVTQKS KQ //