TATC_MYCTU
ID TATC_MYCTU Reviewed; 308 AA.
AC P9WG97; L0T8U4; P66895; Q10702;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatC {ECO:0000255|HAMAP-Rule:MF_00902}; OrderedLocusNames=Rv2093c;
GN ORFNames=MTCY49.33c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=16952959; DOI=10.1128/jb.00631-06;
RA Saint-Joanis B., Demangel C., Jackson M., Brodin P., Marsollier L.,
RA Boshoff H., Cole S.T.;
RT "Inactivation of Rv2525c, a substrate of the twin arginine translocation
RT (Tat) system of Mycobacterium tuberculosis, increases beta-lactam
RT susceptibility and virulence.";
RL J. Bacteriol. 188:6669-6679(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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. Together with
CC TatB, TatC is part of a receptor directly interacting with Tat signal
CC peptides. {ECO:0000255|HAMAP-Rule:MF_00902}.
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_00902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00902};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00902}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth.
CC {ECO:0000269|PubMed:16952959}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00902}.
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DR EMBL; AL123456; CCP44868.1; -; Genomic_DNA.
DR PIR; H70767; H70767.
DR RefSeq; NP_216609.1; NC_000962.3.
DR RefSeq; WP_003410764.1; NZ_NVQJ01000061.1.
DR AlphaFoldDB; P9WG97; -.
DR SMR; P9WG97; -.
DR STRING; 83332.Rv2093c; -.
DR PaxDb; P9WG97; -.
DR DNASU; 888068; -.
DR GeneID; 888068; -.
DR KEGG; mtu:Rv2093c; -.
DR PATRIC; fig|83332.111.peg.2333; -.
DR TubercuList; Rv2093c; -.
DR eggNOG; COG0805; Bacteria.
DR OMA; EMSFLDH; -.
DR PhylomeDB; P9WG97; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0033281; C:TAT protein transport complex; IBA:GO_Central.
DR GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IBA:GO_Central.
DR GO; GO:0043953; P:protein transport by the Tat complex; IBA:GO_Central.
DR HAMAP; MF_00902; TatC; 1.
DR InterPro; IPR019820; Sec-indep_translocase_CS.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; PTHR30371; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
DR TIGRFAMs; TIGR00945; tatC; 1.
DR PROSITE; PS01218; TATC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..308
FT /note="Sec-independent protein translocase protein TatC"
FT /id="PRO_0000098090"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT REGION 277..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 33855 MW; 9FC9B8DC674ECCCE CRC64;
MRAAGLLKRL NPRNRRSRVN PDATMSLVDH LTELRTRLLI SLAAILVTTI FGFVWYSHSI
FGLDSLGEWL RHPYCALPQS ARADISADGE CRLLATAPFD QFMLRLKVGM AAGIVLACPV
WFYQLWAFIT PGLYQRERRF AVAFVIPAAV LFVAGAVLAY LVLSKALGFL LTVGSDVQVT
ALSGDRYFGF LLNLLVVFGV SFEFPLLIVM LNLAGLLTYE RLKSWRRGLI FAMFVFAAIF
TPGSDPFSMT ALGAALTVLL ELAIQIARVH DKRKAKREAA IPDDEASVID PPSPVPAPSV
IGSHDDVT