ID   HSCA_SHEFN              Reviewed;         619 AA.
AC   Q080Q0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, 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=Sfri_2420;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
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   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-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}.
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; CP000447; ABI72265.1; -; Genomic_DNA.
DR   RefSeq; WP_011637874.1; NC_008345.1.
DR   AlphaFoldDB; Q080Q0; -.
DR   SMR; Q080Q0; -.
DR   STRING; 318167.Sfri_2420; -.
DR   PRIDE; Q080Q0; -.
DR   EnsemblBacteria; ABI72265; ABI72265; Sfri_2420.
DR   KEGG; sfr:Sfri_2420; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000684; 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_1000044888"
SQ   SEQUENCE   619 AA;  66430 MW;  EE24C34661E65E74 CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSAQ ALTLPDEQGR HSLPSVVHYG
     ETNVLVGYEA QDKSALDPQN TIVSVKRFMG RSLTDIQSGV HRLPYELHAS ENGLPVFTTP
     MGQVNPIQVS AEILKPLIAR AETTLGGELA GVVITVPAYF DDAQRQGTKD AAELLGVKVL
     RLLNEPTAAA IAYGLDSKQE GVIAIYDLGG GTFDISVLRL NRGVFEVLAT GGDSALGGDD
     FDHLLVSHLQ QAWQITEPGS QLARQLLIEA RRVKEALTDN DSVEASVVMA DKTLTCTVDK
     SLFNELIGAL VKKTIGCCRR TLRDAGVSVD DVIETVMVGG STRVPLVREQ VETFFKKTPL
     TSIDPDRVVA IGAAIQADIL VGNKPESDLL LLDVIPLSLG VETMGGLVEK VVTRNTTIPV
     ARAQEFTTFK DGQTAMAFHV VQGERELVED CRSLARFTLH GIPPLAAGAA HIRVTFQVDA
     DGLLSVTAME KSTGVNTSIQ VKPSFGLSDT EIATMLKDSM KYAKDDITRR MLAEQKVEAA
     RVIESLNAAL AKDAALLDEQ EREELVVAIA QLDAVAQQDN IDAIEKAIAN LDDKTQDFAS
     RRMDNSIRAA LKGQSVDNI