ID   HSCA_ACIB5              Reviewed;         619 AA.
AC   B7I5P9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=AB57_1852;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(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; CP001182; ACJ41231.1; -; Genomic_DNA.
DR   RefSeq; WP_001196578.1; NC_011586.2.
DR   AlphaFoldDB; B7I5P9; -.
DR   SMR; B7I5P9; -.
DR   KEGG; abn:AB57_1852; -.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000007094; 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.
FT   CHAIN           1..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131655"
SQ   SEQUENCE   619 AA;  67838 MW;  D2FC981838EEFFD9 CRC64;
     MALLQIAEPG QSSAPHQHRI AIGIDLGTTH SLVATVLSGK PKVLNDVQNR RLLPSIVHYG
     DNTTHYGEEA KPFIIADPKN TIVSVKRFMG RSKADIKFQH PYELVGSENE MPAFETRAGR
     KTPVEISAEI LKQLKDRAED SLQNPVNGAV ITVPAYFDEA QRQATRDAAQ LAGLNVLRLL
     NEPTAAAVAY GLDQESNLAT DRNYVIYDLG GGTFDVSILR FSQGVFEVLA TGGHTALGGD
     DLDRLIVKWA KKQLNIDVLS DEDYAVFIVA ARQAKEQLST QDSVELKLLE ATLTLDRPTF
     ESIIQVALDK TISVCKRVLR DAKLELTDIQ NVVLVGGSTR SYAVQKAVRE VFAQEPLCTI
     NPDEVVAIGA SITANQLIGN SQDGSLLLDV TPLSLGLETM GGLVERLISR NTAIPVARRQ
     EFTTYQDGQT AMLIHVVQGE RDLVEHCRSL GRFVLHGIPP MTAGQARIEV TFQVDADGLL
     TVSAREATSG VQAHIDIKPS YGLSEADTER LLIEGFQHAE EDKNLRHLKE TKVEAERELE
     SLEQALKVDA DLLDEKQLDA LNSAKESLKA QLEGSDIQAI EHAVQQLKVH SDAFAALRMN
     RHIDHALKGT KLDDWSKSN