ID Q72VF8_LEPIC Unreviewed; 846 AA.
AC Q72VF8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Hemolysin B {ECO:0000313|EMBL:AAS68966.1};
GN Name=tlyB {ECO:0000313|EMBL:AAS68966.1};
GN OrderedLocusNames=LIC_10339 {ECO:0000313|EMBL:AAS68966.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS68966.1, ECO:0000313|Proteomes:UP000007037};
RN [1] {ECO:0000313|EMBL:AAS68966.1, ECO:0000313|Proteomes:UP000007037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS68966.1,
RC ECO:0000313|Proteomes:UP000007037};
RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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DR EMBL; AE016823; AAS68966.1; -; Genomic_DNA.
DR RefSeq; WP_000889241.1; NC_005823.1.
DR AlphaFoldDB; Q72VF8; -.
DR SMR; Q72VF8; -.
DR GeneID; 61143694; -.
DR KEGG; lic:LIC_10339; -.
DR HOGENOM; CLU_005070_4_1_12; -.
DR Proteomes; UP000007037; Chromosome I.
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; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 427..462
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 818..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..102
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 423..480
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 846 AA; 95305 MW; 69DF095B0A4F4349 CRC64;
MLEFTKRAKR VINEIAQDEA KRLGSDYIGP EHILLGLLKE EDSVAIKILN NLNINLNELR
KEVERRTREA SGALLMDVAG GQDRYQKIIE LSKEEAKRLK HNYVGTEHIL LALLRDNNNI
AGGALYSFSV NYNVIKSEIL RLLGAPPTSS VGVSSTTQSG PQPRQEKTKT PILDEFARDL
TQLARDKKLD PVVGRATEIQ RVIQILSRKT KNNPVLVGES GVGKTAIVEG LALAIVEKSV
PDLLFEKRVL SLDLASLIAG TKYRGEFEER LKKIMKEITS STNIIIFIDE LHTLIGAGAA
EGAVDAANIL KPALARGELQ CIGATTSAEY RKYIEKDSAL ERRFQVVKVA EPSVDDAIQI
LQGLKKAYET HHKVRYSDKA LEQSVKLSHR YINDRYLPDK AIDIIDEAGA KARLANCARP
QTIKDLEEEI KSLASKKEEL VRAQEYEKAA GVRDEVNRKK QAMEEKLRSW QEKMEDFAVN
IEEDDILSVI SLWTGIPLEK MEESESDKLL RLEEELKKRV VGQAEAIEKI AKAVRRARTG
FKSERRPTGS FIFLGPTGVG KTELAKALAN FLFGNDDAML RVDMSEYMEP HAVSRLIGAP
PGYVGYDDGG QLTEFVRKRP YSIILLDEIE KAHHDIFNIL LQIMEEGNLT DTKGRKVNFR
DTIIIMTSNI GAKEIQAGGR LGFEDRKDEA LKYKSDQTRD QLKKYFNPEF LNRVDEVIYF
GSLTKENIMS IIDIMVTDTN KRLHEKTIQI SITQAAKNHI MDIGYDEKFG ARPLRRVFQR
ELEDHMAVQT LKGAYKEPTK IEIDFKEGKL EFLETPWTDY KPVDPKTGGN DNSSGNPERS
EEIALV
//
