ID   HSCA_SHEAM              Reviewed;         619 AA.
AC   A1S548;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Sama_1297;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000507; ABL99504.1; -; Genomic_DNA.
DR   RefSeq; WP_011759413.1; NC_008700.1.
DR   AlphaFoldDB; A1S548; -.
DR   SMR; A1S548; -.
DR   STRING; 326297.Sama_1297; -.
DR   EnsemblBacteria; ABL99504; ABL99504; Sama_1297.
DR   KEGG; saz:Sama_1297; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009175; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044884"
SQ   SEQUENCE   619 AA;  65848 MW;  ED100907674FCC64 CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGE ARTLADAQGR HSLPSIVRYA
     KEGISVGQEA ELHSATDAAN TIVSVKRFMG RSLADIEAGS QRFPYQFSAS ENGLPLFNTP
     QGQVNPVQVS AEILRPLIAR AEDTLGGSLE GAVITVPAYF DDAQRQGTKD AAQLLGVKVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL NRGVFEVLAT GGDSALGGDD
     FDHLLGGYLA QQWGLDLADT GLGRKLMIEA RRVKEALTET DTVTATLEYQ GQAYHHDIDR
     GTFDALIAAL VKKTIAACRR ALRDAGIDAG EVLETVMVGG STRVPLVRSE VEAFFGKAPL
     TSIDPDRVVA IGAAIQADIL VGNKPESDLL LLDVIPLSLG IETMGGLVEK IVSRNTTIPV
     ARAQEFTTFK DGQTAMAFHV VQGERELVQD CRSLARFTLK GIPPLAAGAA HIRVTFQVDA
     DGLLSVTAME KSTGVKSSIQ VKPSFGLSDT EIATMLKDSM KHAKEDISRR MLAEQQVEAA
     RVLESLHSAL AKDKVLLSEE ELNDITAAMA ELAEVAKGDD ADAILAAIER LDNQTQEFAA
     KRMDNSIRNA LKGQSVDTI