HSCA_ACIAD
ID HSCA_ACIAD Reviewed; 620 AA.
AC Q6FCE6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=ACIAD1399;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG68265.1; -; Genomic_DNA.
DR RefSeq; WP_004925600.1; NC_005966.1.
DR AlphaFoldDB; Q6FCE6; -.
DR SMR; Q6FCE6; -.
DR STRING; 62977.ACIAD1399; -.
DR EnsemblBacteria; CAG68265; CAG68265; ACIAD1399.
DR GeneID; 45233814; -.
DR KEGG; aci:ACIAD1399; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; ASP62977:ACIAD_RS06460-MON; -.
DR Proteomes; UP000000430; 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; Reference proteome.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_0000078613"
SQ SEQUENCE 620 AA; 68321 MW; E2C35AF54714285C CRC64;
MALLQIAEPG QSSAPHEHRI AIGIDLGTTH SLVATVLSGQ SKVLQDEKGR VLFPSIVHYA
EQSIEYGDDA KPFITTDPKN SIISVKRFMG RSKADIKFQH PYVLVGNDNE MPAFETAQGR
KTPVEISAAI LNQLKIRAEE SLKNPINGAV ITVPAYFDEA QRQATRDAAQ LAGLNVLRLL
NEPTAAAIAY GLDQENQLSS DRNYVIYDLG GGTFDVSILR FSQGVFEVLA TGGHTALGGD
DLDRLIVKWA KKQLHIESLD DHEYAAFLVA ARTAKEQLSE QQSVYFKALD HKLELNRDTF
ESIIQIALDK TISVCKRVLR DAKLSLDEIE KVVLVGGSTR SYAVQNVVRQ VFNQEPLCTI
NPDEVVAIGA SITANQLIGN SQDGSLLLDV TPLSLGLETM GGLVERLISR NTAIPVARRQ
EFTTYQDGQS AMLIHVVQGE RDLVEHCRSL GRFVLHGIPP MTAGQARIEV TFQVDADGLL
TVSAQETTSG VKAQIDIKPS YGLSATDTER LLLEGFQHAE EDKNLRHLQE TKVEAQRELE
ALEQALKNDA GLLDIQQLQA LHTAKDQLQQ QLQSNDIDQI ERAVAQLKIH SDEFAALRMN
QHIDHALKGT KLEDWSDSQK
