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Database: UniProt
Entry: X2JTX5_AGGAC
LinkDB: X2JTX5_AGGAC
Original site: X2JTX5_AGGAC 
ID   X2JTX5_AGGAC            Unreviewed;       254 AA.
AC   X2JTX5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000256|HAMAP-Rule:MF_00902};
GN   Name=tatC {ECO:0000256|HAMAP-Rule:MF_00902};
GN   ORFNames=CF65_01152 {ECO:0000313|EMBL:AHN71572.1};
OS   Aggregatibacter actinomycetemcomitans HK1651.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=272556 {ECO:0000313|EMBL:AHN71572.1, ECO:0000313|Proteomes:UP000019758};
RN   [1] {ECO:0000313|EMBL:AHN71572.1, ECO:0000313|Proteomes:UP000019758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK1651 {ECO:0000313|EMBL:AHN71572.1,
RC   ECO:0000313|Proteomes:UP000019758};
RA   Gillaspy A.F., Griffin J., Najar F., Hinkle J., Lewis L.A.,
RA   McLaughlin R.E., Hartman K., Nydick C., Gipson M., Conway B., Vaughn J.,
RA   Thompson C., Gipson J., Maddera L., Carson M., Kenton S., Lai H., Roe B.A.,
RA   Orvis J., Zaitshik J., Griffin J., Scott E., Dyer D.W.;
RT   "Genome sequencing and closure of the periodontal pathogen, Aggregatibacter
RT   actinomycetemcomitans.";
RL   Submitted (MAR-2014) 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       TatB, TatC is part of a receptor directly interacting with Tat signal
CC       peptides. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00902}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00902}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00902}.
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DR   EMBL; CP007502; AHN71572.1; -; Genomic_DNA.
DR   RefSeq; WP_005545082.1; NZ_CP007502.1.
DR   AlphaFoldDB; X2JTX5; -.
DR   SMR; X2JTX5; -.
DR   GeneID; 77211106; -.
DR   KEGG; aah:CF65_01152; -.
DR   PATRIC; fig|272556.10.peg.806; -.
DR   eggNOG; COG0805; Bacteria.
DR   HOGENOM; CLU_031942_1_1_6; -.
DR   Proteomes; UP000019758; 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   HAMAP; MF_00902; TatC; 1.
DR   InterPro; IPR019820; Sec-indep_translocase_CS.
DR   InterPro; IPR002033; TatC.
DR   NCBIfam; TIGR00945; tatC; 1.
DR   PANTHER; PTHR30371; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC; 1.
DR   PANTHER; PTHR30371:SF0; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00902; TatC; 1.
DR   PRINTS; PR01840; TATCFAMILY.
DR   PROSITE; PS01218; TATC; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00902};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_00902};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00902};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00902}; Transport {ECO:0000256|HAMAP-Rule:MF_00902}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        117..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        158..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        196..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
SQ   SEQUENCE   254 AA;  28347 MW;  469EF6954AD2CC50 CRC64;
     MTSVDDTQPL ITHLVELRTR LLRSIIFVAV VFVALVYFSN EIYNFVAAPL TANLPNGSSM
     IATNIATPFF TPIKLTGVVA VFISVPYLLY QIWAFVAPAL YQHEKRLIYP LLFSSTVLFY
     LGVAFAYYVV FPLVFSFLTK TAPEGVAIAT DISSYLDFVL TLFLAFGVCF EVPVAIILLC
     WTGVTTPEDL RSKRPYIIVA AFFIGMLLTP PDVFSQTLLA APMCLLFEVG VLCARFYRPR
     EDDETQNESD SAKQ
//
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