ID   HSCA_MANSM              Reviewed;         616 AA.
AC   Q65RT2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=MS1721;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(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; AE016827; AAU38328.1; -; Genomic_DNA.
DR   RefSeq; WP_011200889.1; NC_006300.1.
DR   AlphaFoldDB; Q65RT2; -.
DR   SMR; Q65RT2; -.
DR   STRING; 221988.MS1721; -.
DR   EnsemblBacteria; AAU38328; AAU38328; MS1721.
DR   KEGG; msu:MS1721; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000607; 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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078631"
SQ   SEQUENCE   616 AA;  66945 MW;  ED4EBDCBC84B9E02 CRC64;
     MALLQIAEPG LMAAPHQHKL AVGIDLGTTN SLVATVRSAH TEILLDEKDR PLVPSIVHFG
     DNNEITVGYE AGELASIDPQ NTVISVKRLI GRSLEDVQAR YPNLPYRFEA SENGLPLIST
     RKSAVSPVEV SSEILKKLTA LAKRRLGGEL QGAVITVPAY FDDAQRQSTK DAAKLAGLNV
     LRLLNEPTAA AIAYGLDSGK EGVIAVYDLG GGTFDISILR LSKGVFEVLA TGGDTALGGD
     DFDHLVADWI TEQSGISPQD DKQKRQLVEL ATRLKIQLTD NETVAIQYQN WHGKISRNQF
     NQLIQPLVKR SLISCRRALK DANVTADEVN EVVMVGGSTR VPFVREQVGE FFKRQPLTSI
     DPDKVVALGA AVQADILVGN KPDSEMLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVARA
     QEFTTFKDGQ TAMTVHIVQG EREMVADCRS LARFTLRGIP PMAAGAAQVR VTYQVDADGL
     LNVTAMEKST GVQSSIQVKP SYGLTDDEIT QMLKASMDNA KQDIDARLLA EQRVEAKRVI
     ESVLSALSHD RDLLNDEELS AIKKALVELD KLQQQNDTLA IKQGIKDLDA ATQEFAARRM
     DKSIRSALTG HSVEDI