TATCY_BACSU
ID TATCY_BACSU Reviewed; 254 AA.
AC O05523;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sec-independent protein translocase protein TatCy {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatC2 {ECO:0000255|HAMAP-Rule:MF_00902}; Synonyms=tatCy, ydiJ;
GN OrderedLocusNames=BSU05990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP IDENTIFICATION OF THE TAT GENES.
RX PubMed=11007775; DOI=10.1074/jbc.m004887200;
RA Jongbloed J.D.H., Martin U., Antelmann H., Hecker M., Tjalsma H.,
RA Venema G., Bron S., van Dijl J.M., Mueller J.;
RT "TatC is a specificity determinant for protein secretion via the twin-
RT arginine translocation pathway.";
RL J. Biol. Chem. 275:41350-41357(2000).
RN [4]
RP EXPORT OF THE YWBN PROTEIN, AND CHARACTERIZATION OF THE TWO TAT TRANSLOCASE
RP SYSTEMS.
RX PubMed=15554971; DOI=10.1111/j.1365-2958.2004.04341.x;
RA Jongbloed J.D.H., Grieger U., Antelmann H., Hecker M., Nijland R., Bron S.,
RA van Dijl J.M.;
RT "Two minimal Tat translocases in Bacillus.";
RL Mol. Microbiol. 54:1319-1325(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19049517; DOI=10.1111/j.1742-4658.2008.06776.x;
RA Barnett J.P., van der Ploeg R., Eijlander R.T., Nenninger A., Mendel S.,
RA Rozeboom R., Kuipers O.P., van Dijl J.M., Robinson C.;
RT "The twin-arginine translocation (Tat) systems from Bacillus subtilis
RT display a conserved mode of complex organization and similar substrate
RT recognition requirements.";
RL FEBS J. 276:232-243(2009).
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. Required for
CC YwbN secretion. {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:19049517}.
CC -!- SUBUNIT: Forms a complex with TatAy. Two types of complexes exist: one
CC composed of TatAy and TatCy, and another composed only of TatAy.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:19049517}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:19049517}.
CC -!- MISCELLANEOUS: B.subtilis possesses two minimal, substrate-specific,
CC Tat translocases: TatAd-TatCd and TatAy-TatCy, each one composed of a
CC TatA and a TatC protein. TatA is bifunctional and performs the function
CC of both the TatA and TatB proteins of Gram-negative organisms.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00902}.
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DR EMBL; D88802; BAA19723.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12418.1; -; Genomic_DNA.
DR PIR; C69787; C69787.
DR RefSeq; NP_388480.1; NC_000964.3.
DR RefSeq; WP_010886426.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O05523; -.
DR SMR; O05523; -.
DR IntAct; O05523; 22.
DR STRING; 224308.BSU05990; -.
DR TCDB; 2.A.64.3.2; the twin arginine targeting (tat) family.
DR PaxDb; O05523; -.
DR PRIDE; O05523; -.
DR EnsemblBacteria; CAB12418; CAB12418; BSU_05990.
DR GeneID; 938010; -.
DR KEGG; bsu:BSU05990; -.
DR PATRIC; fig|224308.43.peg.629; -.
DR eggNOG; COG0805; Bacteria.
DR InParanoid; O05523; -.
DR OMA; RMLNYSA; -.
DR PhylomeDB; O05523; -.
DR BioCyc; BSUB:BSU05990-MON; -.
DR Proteomes; UP000001570; Chromosome.
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..254
FT /note="Sec-independent protein translocase protein TatCy"
FT /id="PRO_0000098096"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
SQ SEQUENCE 254 AA; 29056 MW; 803DC23BCB6B24A7 CRC64;
MTRMKVNQMS LLEHIAELRK RLLIVALAFV VFFIAGFFLA KPIIVYLQET DEAKQLTLNA
FNLTDPLYVF MQFAFIIGIV LTSPVILYQL WAFVSPGLYE KERKVTLSYI PVSILLFLAG
LSFSYYILFP FVVDFMKRIS QDLNVNQVIG INEYFHFLLQ LTIPFGLLFQ MPVILMFLTR
LGIVTPMFLA KIRKYAYFTL LVIAALITPP ELLSHMMVTV PLLILYEISI LISKAAYRKA
QKSSAADRDV SSGQ
