ID   HSCA_LARHH              Reviewed;         619 AA.
AC   C1D4P9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=LHK_02861;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO75840.1; -; Genomic_DNA.
DR   RefSeq; WP_012698303.1; NC_012559.1.
DR   AlphaFoldDB; C1D4P9; -.
DR   SMR; C1D4P9; -.
DR   STRING; 557598.LHK_02861; -.
DR   PRIDE; C1D4P9; -.
DR   EnsemblBacteria; ACO75840; ACO75840; LHK_02861.
DR   KEGG; lhk:LHK_02861; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002010; 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..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000147717"
SQ   SEQUENCE   619 AA;  66079 MW;  B2D7CE5F21F1E321 CRC64;
     MALLQIAEPG LSAAPHQHRL AVGIDLGTTN SLVATVRSGA ATVLPDEHGY HLLPSVVRYT
     EDGATEVGYA ARAHQSDDPH NTVVSVKRFM GRGLSDLADA AATPYRFVDA PGMVRLVTRQ
     GEKSPVEVSA DILRALKARA ESSLGGELTG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
     LLNEPTAAAI AYGLDNAAEG TYVVYDLGGG TFDVSILRLT RGVFEVLATS GDSALGGDDF
     DHRIYCWLLE KAGLSQLPDG DIRRLLTLAR AAKEHLTDNT SARINTVLSD RQVIDLELSR
     DELAAITRTL VDKTLLPVRR ALRDARISVD DVKGVVLVGG ATRMPQVRRA VGDFFKRPPL
     TNLDPDQVVA IGAAMQANVL AGNKGEDDWL LLDVTPLSLG LETMGGLVEK IIPRNSTIPT
     ARAQEFTTFK DGQTAMAVHV LQGERELVSD CRSLARFELR GIPPMVAGAA RIRVTFQVDA
     DGLLSVAARE QSSGVEASIT IKPSYGLTDD QITQMLTDSL AHVKDDIAAR KLREAVVDAE
     SLIATTDAAL KSDGDLLAPS ELQAIDNAVA ALRSAIAAQQ TVAINAATAR LNDATNDFAS
     RRMDRNIRRA LAGQKISDL