ID   HSCA_ACIBS              Reviewed;         620 AA.
AC   B0VNV8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=ABSDF1849;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP01186.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VNV8; -.
DR   SMR; B0VNV8; -.
DR   EnsemblBacteria; CAP01186; CAP01186; ABSDF1849.
DR   KEGG; abm:ABSDF1849; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001741; 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; Stress response.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131657"
SQ   SEQUENCE   620 AA;  68015 MW;  79148A2DCACC7FC3 CRC64;
     MPLLQIAEPG QSSAPHQHRI AIGIDLGTTH SLAATVLSGK PKVLNDVQNR RLLPSIVHYG
     DNTTHYGEEA KPFIIADPKN TIVSVKRFMG RSKADIKFQH PYELVGSEKN EMPAFETRAG
     RKTPVEISAE ILKQLKDRAE DSLQNPVNGA VITVPAYFDE AQRQATRYAA QLAGLNILRL
     LNEPTAAAVA YGLDQESNLA TDRNYVIYDL GGGTFDVSIL RFSQGVFEVL ATGGHTALGG
     DDLDRLIVKW AKKQLNIDVL SDEDYAVFIV AARQAKEQLS TQDSVELKLL EATLTLDRPT
     FESIIQVALD KTISVCKRVL RDAKLELTDI QNVVLVGGST RSYAVQKAVR EVFAQEPLCT
     INPDEVVAIG ASITANQLIG NSQDGSLLLD VTPLSLGLET MGGLVERLIS RNTAIPVARR
     QEFTTYQDGQ TAMLIHVVQG ERDLVEHCRS LGRFVLHGIP PMTAGQARIE VTFQVDADGL
     LTVSAREATS GVQAHIDIKP SYGLSEADTE RLLIEGFQHA EEDKNLRHLK ETKVEAEREL
     EALEQALKVD ADLLDEKQLE ALNSAKESLK AQLEGSDIQA IEQAVQQLKV HSDAFAALRM
     NRHIDHALKG TKLDDWSKSN