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Database: UniProt
Entry: D2THU1_CITRI
LinkDB: D2THU1_CITRI
Original site: D2THU1_CITRI 
ID   D2THU1_CITRI            Unreviewed;       900 AA.
AC   D2THU1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=T6SS protein Cts1V {ECO:0000313|EMBL:CBG89524.1};
GN   Name=cts1V {ECO:0000313|EMBL:CBG89524.1};
GN   OrderedLocusNames=ROD_27811 {ECO:0000313|EMBL:CBG89524.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89524.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG89524.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG89524.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FN543502; CBG89524.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2THU1; -.
DR   STRING; 637910.ROD_27811; -.
DR   KEGG; cro:ROD_27811; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_2_0_6; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          13..154
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          529..556
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   900 AA;  98413 MW;  F96EF4D5DAF69EC6 CRC64;
     MSLVVAITRK NLFGKLNISL FKSVESATTL CKLRGNPYVE LVHWLNQIYQ QQDSDIRHIV
     RHFELDAEIL ERDFAQALTR LPAGASSISD FSYHIELAIE RAWIFASLEC QNTSIRSGHL
     LMALLTTMEL RRALFSISSV FEKIPLEQLS KDLGYIIRDS AEESEAGGAM VSAEAGVPGE
     ASNAMGGTQS GGLAQYSTDL TALAREGKID PVLGRDKEIN TMIDILLRRR QNNPLLTGEA
     GVGKTAVVEG LALALAAGEV PPALQKVRLL TLDVTALSAG ASMKGEFEAR LKAVLEDAAK
     SVDPVILFID EVHTLVGAGG NAGTGDAANL MKPMLARGQL RTIGATTWSE FKRHIEKDPA
     LTRRFQVLQV EEPSEDLAIA MLRGLLPVLE KHHGVWVMDE AIRAAVRLSH RYIPARQLPD
     KAISLLDTAC ARVAVAQHAP PTELQLLKFH QQSAQAELSM LEKAIGFGKE DDKRLQPIQR
     AIDDHAEEAT ALERRWAQEC ELVATIIDTR QQLLAATVDD PQTPEAEKIS YLQSRLNELE
     ATLSEIRGEK ALVQTEVNAS IVAAIVADWT GIPVGQVLKD DVSAVMELPQ RLAEKVIGQT
     YALTCLSQSI QTARAGLADP QKPFGVFMLV GPSGVGKTET ALAIADQLYG GKQNLITINM
     SEYQEAHTVS SLKGSPPGYV GYGEGGVLTE AVRRKPYSVI LLDEVEKAHT DVHELFFQVF
     DKGSMEDGEG RQIDFRNTVI LLTSNAGSDI ISSACADPQT MPDEEGLLKL LQPALLKIFP
     AAFLGRVTVI PYLPLATDSL QHIVRIHLNR IAERAKAQYE MTLNFSDELV QHVVEQCPVA
     ETGARMLIRF IEKNILPKIG SALLTQADKP AKNKTITMQC ILSEEKEIDI EMQLEGKQNI
//
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