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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//