ID   HSCA_NEIMB              Reviewed;         620 AA.
AC   Q9JS04;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=NMB1169;
GN   and
GN   OrderedLocusNames=NMB1131;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41554.1; -; Genomic_DNA.
DR   EMBL; AE002098; AAF41519.1; -; Genomic_DNA.
DR   PIR; B81118; B81118.
DR   RefSeq; NP_274160.1; NC_003112.2.
DR   RefSeq; NP_274196.1; NC_003112.2.
DR   RefSeq; WP_002244129.1; NC_003112.2.
DR   AlphaFoldDB; Q9JS04; -.
DR   SMR; Q9JS04; -.
DR   STRING; 122586.NMB1131; -.
DR   PaxDb; Q9JS04; -.
DR   EnsemblBacteria; AAF41519; AAF41519; NMB1131.
DR   EnsemblBacteria; AAF41554; AAF41554; NMB1169.
DR   KEGG; nme:NMB1131; -.
DR   KEGG; nme:NMB1169; -.
DR   PATRIC; fig|122586.8.peg.1434; -.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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_0000078635"
SQ   SEQUENCE   620 AA;  66166 MW;  7B4C06AD48AA4E8F CRC64;
     MALLQISEPG MSAAPHRHRL AAGIDLGTTN SLVATVRSGS AACLPDAEGR VTLPSVVRYL
     ENGGIEVGKT ALSAQKTDPL NTVSSAKRLI GRTLADLHQN THYLPYRFGD NQRVIELHTR
     QGVKTPVEVS AEILKTLKSR AEETLGGDLV GVVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA IAYGLDNASE GTFVVYDLGG GTFDVSVLQL TKGLFEVKAT GGNSALGGDD
     FDHRLFCRLL EQNGLSQLNE QDSQLLLSLV RAAKEQLTTQ TEARIQATLS DGMAIDTSIS
     RAEFHNLTQH LVMKTLEPVT QALKDAGVGK NEVKGVIMVG GSTRMLHVQQ AVATFFGQTP
     LNNLNPDEVV ALGAAIQANV LAGNKTDGEW LLLDVTPLSL GLETYGGLAE KIIPRNSTIP
     TARAQDFTTF KDGQTAMTIH VVQGERELVA DCRSLAKFTL RGIPPMAAGA ARIRVTFQID
     ADGLLSVSAQ EQSTGVQAQI EVKPSYGLDD DTITQMLKDS MSNAAEDMAA RARAEAVVEA
     ESLTDAVNAA LELDSDLLDA EELQQIRQGI ADLQGRLKDG KAEDIRAAAA KLGSITDNFA
     AKRMNRNIQR ALTGQSVDNI