ID   HSCA_VESOH              Reviewed;         614 AA.
AC   A5CWM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=COSY_0528;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Vesicomyosocius.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA   Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT   clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
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:0000255|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; AP009247; BAF61646.1; -; Genomic_DNA.
DR   RefSeq; WP_011929916.1; NC_009465.1.
DR   AlphaFoldDB; A5CWM2; -.
DR   SMR; A5CWM2; -.
DR   STRING; 412965.COSY_0528; -.
DR   EnsemblBacteria; BAF61646; BAF61646; COSY_0528.
DR   KEGG; vok:COSY_0528; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000247; Chromosome.
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; 2.60.34.10; -; 1.
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   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01991; HscA; 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; Chaperone; Nucleotide-binding.
FT   CHAIN           1..614
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044901"
SQ   SEQUENCE   614 AA;  67355 MW;  34E315D09DFF71D7 CRC64;
     MTLLQISEPS QVSKPHQHKL VIGIDLGTTN SLVASVINGQ SKVIMDENNE AVLPSIIHCG
     KHNKLTVGCD AYPYAKTDPT NTIISIKRFM GMSYEEVSTF KNCPYQLIKD GNNVLFHTSM
     GNLSAVEISA SILSSLKQRA ENSLGGVLSG AVITTPAYFN DAQRQATKDA ATLAGLKTLR
     LLNEPTAAAV AYGLESGEEG VHAIYDLGGG TFDISILNFS KGVFKVLAIG GDATLGGDDF
     DELIINDCIE QLSINELTPA QMQEIKQFSR IAKETLSNYE FSEFDCIKRP YCITKKKFET
     LAKVLIKRTL LLTKQAIRDA QVDVKNIKNI IMVGGSTRIP LVCSMVSDLF NKPVLCSINP
     DEVVAKGAAI QANILAGIKS QNDILLLDVL PLSLGLETMG GLVEKIIHRN TTIPIIRAQE
     FTTFKDGQTA MSIHVLQGER ELVRDCRSLA KFDLYGIPAM VAGNARIRIE FQVDVDGLLS
     VSAVEQISGV KTNISIKPSY GLTDVQKEKM LKDSFLFAKT DIQTRKLHET QVEANRTIEA
     IDSAIKKDKN MLDDKMLNNI LNARNTLFDI VHSDDEKAIS IAIENLENSC LKFVEMRMNS
     SVMKAIQGRN IDEF