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Database: UniProt
Entry: C6HVK3_9BACT
LinkDB: C6HVK3_9BACT
Original site: C6HVK3_9BACT 
ID   C6HVK3_9BACT            Unreviewed;       612 AA.
AC   C6HVK3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   28-JUN-2023, entry version 31.
DE   SubName: Full=Chaperone protein HscA {ECO:0000313|EMBL:EES53362.1};
GN   ORFNames=UBAL3_79320011 {ECO:0000313|EMBL:EES53362.1};
OS   Leptospirillum ferrodiazotrophum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53362.1, ECO:0000313|Proteomes:UP000009374};
RN   [1] {ECO:0000313|EMBL:EES53362.1, ECO:0000313|Proteomes:UP000009374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA   Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA   Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA   Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT   "Community genomic and proteomic analyses of chemoautotrophic iron-
RT   oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT   ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL   Appl. Environ. Microbiol. 75:4599-4615(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; GG693864; EES53362.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HVK3; -.
DR   Proteomes; UP000009374; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10170; HSP70_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009374}.
SQ   SEQUENCE   612 AA;  66294 MW;  7FE415F07505A3EB CRC64;
     MKHVIGIDLG TTHSLVAYRK EDGTVEVIRD REGRSLLPSV VALSPDGVRV GWTARELIND
     PQTTVVYAAK RLMGRSFAET AAERAHLAYP VIDKNGTPAI PDPARHRSLT PPEIGSLILA
     NLRSRAEEAL GCEVTEAVIT VPAYFNDGQR QATKDAGALA GLNVLRIINE PTAAALAYGL
     GEKKDGLFAI FDLGGGTFDF SLLEIRKGIF EVRATNGDTH LGGEDFDRAI MESWFSEIPG
     LRELAIRSEV RDTLRKEAER AKIVLSRDTS VAVNIPSLNL STTLTRERLN SLVEPFVERA
     FASVRAAMRD SDTDPKSVDG VILVGGSTRL LRFREAVSDY FGATLYDSVD PDLVVAEGAA
     VQADILSGRR KDLLLLDVTP LSLGIETIGG VMSTLIPRNT TIPAQAKELF TTYVDGQVNV
     DIHVLQGERE MAADNRSLGR FTLSGIPPLP AGAPRIEVTF QIDANGILEV TAREQTTGQR
     ANVVIHPSYG LGKDDVRELL KEAFAHAKDD FALRLLIDSR TEAQTVLGAT ERALGTVGDD
     ILGSEERSAI TEQMKVLRSA MEGSDGKKVR DEIRNLDRLT QPLAERLVNR SLTEALSGKA
     LPELPKEGGS HA
//
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