HSCA_ACIB3
ID HSCA_ACIB3 Reviewed; 619 AA.
AC B7H3H4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=ABBFA_001869;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
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; CP001172; ACJ58926.1; -; Genomic_DNA.
DR RefSeq; WP_001196578.1; NZ_CP001172.1.
DR AlphaFoldDB; B7H3H4; -.
DR SMR; B7H3H4; -.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000006924; 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_1000131654"
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