ID   HSCA_ACIBT              Reviewed;         619 AA.
AC   A3M561;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=A1S_1628;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO12055.2; -; Genomic_DNA.
DR   RefSeq; WP_001196570.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M561; -.
DR   SMR; A3M561; -.
DR   KEGG; acb:A1S_1628; -.
DR   HOGENOM; CLU_005965_2_3_6; -.
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..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131658"
SQ   SEQUENCE   619 AA;  67711 MW;  9A6FFA0F66B6D209 CRC64;
     MALLQIAEPG QSSAPHQHRI AIGIDLGTTH SLVATVLSGK PKVLNDVQNR RLLPSIVHYG
     DNTTHYGEEA KPFIIADPKN TIVSVKRFMG RSKADIKFQH PYELVGSENE MPAFETRAGR
     KTPVEISAEI LKQLKARAED 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
     ALEQALKVDA DLLDEKQLEA LNSAKGSLKA QLEGSDIQAI EQAVQQLKVH SDAFAALRMN
     RHIDHALKGT KLDDWSKSN