ID   HSCA_METFK              Reviewed;         622 AA.
AC   Q1H365;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Mfla_0804;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
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   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-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; CP000284; ABE49072.1; -; Genomic_DNA.
DR   RefSeq; WP_011479169.1; NC_007947.1.
DR   AlphaFoldDB; Q1H365; -.
DR   SMR; Q1H365; -.
DR   STRING; 265072.Mfla_0804; -.
DR   PRIDE; Q1H365; -.
DR   EnsemblBacteria; ABE49072; ABE49072; Mfla_0804.
DR   KEGG; mfa:Mfla_0804; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002440; 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; Reference proteome.
FT   CHAIN           1..622
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044865"
SQ   SEQUENCE   622 AA;  66836 MW;  E6B26A2D76D23EAA CRC64;
     MALLQISEPG QSTAPHQHRL AVGIDLGTTN SLVATVRSGL STVLLDEAGK ALLPSVVHYA
     ANGQVEVGYA AQRQQSHDPQ NTIASAKRFL GRGLNDIGDT SHLPYQFVDV PGMVQIETRA
     GIKSPVEISA EILKSLKARA EQALGGELTG AVITVPAYFD DAQRQATKDA ARIAGINVLR
     LLNEPTAAAI AYGLDNASEG IYVVYDLGGG TFDVSILRLT KGVFEVLSTN GDSALGGDDF
     DRRIFHWILE QTHLQAPNPA DTRLLMTASK EAKEWLTEHT SANIAVTLSN GKTVDLSLSR
     TEFHSLTQPL LNRTLVPIRK ALRDASLTVK EVKGIVLVGG ATRMPQVQQA VADFFGQAPL
     TNLDPDQVVA LGAAIQANIL AGNRHDDELL LLDVIPLSLG LETMGGLVEK IIPRNSTLPI
     ARAQDFTTFK DGQTAMSIHV LQGEREMVAD CRSLGRFELR GIPPMAAGAA RIRVTFQVDA
     DGLLSVSAQE QTSGAHANIV VKPSYGLSEE QITNMLQASF TAAEADKHAR ALQEARVDAA
     RLLEALEAAL RQDGDKLLND EERTEITRQM EHLRNIAQHE DSDAINKAVD ALNHATETFA
     ARRMDASVKQ ALAGQSLNTL DI