ID   A0A1A6C7U2_9GAMM        Unreviewed;       623 AA.
AC   A0A1A6C7U2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN   ORFNames=Thpro_020354 {ECO:0000313|EMBL:OBS10638.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS10638.1, ECO:0000313|Proteomes:UP000029273};
RN   [1] {ECO:0000313|EMBL:OBS10638.1, ECO:0000313|Proteomes:UP000029273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS10638.1,
RC   ECO:0000313|Proteomes:UP000029273};
RX   PubMed=25342676;
RA   Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA   Watkin E.;
RT   "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT   'Thiobacillus prosperus' Type Strain DSM 5130.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-
CC       containing proteins. Has a low intrinsic ATPase activity which is
CC       markedly stimulated by HscB. {ECO:0000256|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679,
CC       ECO:0000256|RuleBase:RU003322}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS10638.1}.
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DR   EMBL; JQSG02000001; OBS10638.1; -; Genomic_DNA.
DR   RefSeq; WP_065089122.1; NZ_JQSG02000001.1.
DR   AlphaFoldDB; A0A1A6C7U2; -.
DR   STRING; 160660.BJI67_07165; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000029273; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd10236; HscA_like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00679; HscA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042039; HscA_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA.
DR   NCBIfam; TIGR01991; HscA; 1.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00679};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00679}; Reference proteome {ECO:0000313|Proteomes:UP000029273}.
SQ   SEQUENCE   623 AA;  66500 MW;  E64E06AACF17E691 CRC64;
     MSLLQIAEPG MSTAPHAHRL AAGIDLGTTN SLVASVRSGV AETLADEAGR HILPSVVRYR
     ADGEPIVGAA AKMDAADDPL NTLASIKRLM GRGVDDLKTL AGHVPYRFAP GESVVPRIRT
     DAGDVTAVEV SAEILRSLRA RAEAALGGEL AGVVITVPAY FDDAQRQATK DAARLAGLNV
     FRLLNEPTAA AVAYGLDQGG DGLIAVYDLG GGTFDISILR LNRGVFEVLA TGGDSALGGD
     DFDREIAAWI MAEAGLGGDA DHRTMRRLMR EACAAKEALT EVESVGITLD LGDERHWQGH
     LTREQLDTLL DPLIQKTLAA CRRALRDAGV EREAIGDVVM VGGSTRVPRV RERVASFFGR
     APRVDIDPDK VVAVGAAIQA DVLAGNKPDG ELLLLDVIPL SLGIETMGGL VEKIIPRNTT
     IPVARAQEFT TFKDGQGAMA IHVLQGEREL VDDCRSLARF VLSGLPPMVA GAPRIRVTFQ
     VDADGLVGVT AEELTSGVQA GVEIKPSYGL EEEEIERMLR ASIEHARDDM LARRLREEQV
     EADRVIEALD AALATDGERL LSEHERTVIL SAREALVRCR DSGDPEAIRS AIEAVEHASS
     DFVARRMDTA ISSAMSGHRV DEF
//