ID   HSCA_NEIMA              Reviewed;         620 AA.
AC   Q9JUF4; A1IRW9;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=NMA1340;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(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; AL157959; CAM08517.1; -; Genomic_DNA.
DR   PIR; A81903; A81903.
DR   RefSeq; WP_002246940.1; NC_003116.1.
DR   AlphaFoldDB; Q9JUF4; -.
DR   SMR; Q9JUF4; -.
DR   EnsemblBacteria; CAM08517; CAM08517; NMA1340.
DR   KEGG; nma:NMA1340; -.
DR   HOGENOM; CLU_005965_2_3_4; -.
DR   OMA; PDPHQRR; -.
DR   BioCyc; NMEN122587:NMA_RS06700-MON; -.
DR   Proteomes; UP000000626; 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..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078634"
SQ   SEQUENCE   620 AA;  66292 MW;  AE81130F2AF92FFC 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 DGMPIDTSIS
     RAEFHNLTQH LVMKTLEPVT QALKDAGVGK NEVKGVIMVG GSTRMLHVQQ AVATFFGQTP
     LNNLNPDEVV ALGAAIQANV LAGNKTDGEW LLLDVTPLSL GLETYGGLAE KIIPRNSTIP
     TARAQDFTTF KDGQTAMTIH VVQGERELVS DCRSLAKFTL RGIPPMAAGA ARIRVTFQID
     ADGLLSVSAQ EQSTGVQAQI EVKPSYGLDD GAITRMLKDS MDNAAEDMAA RARAEAVVEA
     ESLTDAVNAA LELDSDLLDA KELQQIRQGI ADLQGRLKDG KAEDIRSAVA KLSRSTDNFA
     AKRMNRNIQR ALTGQSVDNI