ID   HSCA_NEIG1              Reviewed;         620 AA.
AC   Q5F8E8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=NGO0829;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW89539.1; -; Genomic_DNA.
DR   RefSeq; WP_010951132.1; NC_002946.2.
DR   RefSeq; YP_207951.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8E8; -.
DR   SMR; Q5F8E8; -.
DR   STRING; 242231.NGO_0829; -.
DR   EnsemblBacteria; AAW89539; AAW89539; NGO_0829.
DR   KEGG; ngo:NGO_0829; -.
DR   PATRIC; fig|242231.10.peg.978; -.
DR   HOGENOM; CLU_005965_3_0_4; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000535; 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; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078633"
SQ   SEQUENCE   620 AA;  66421 MW;  D442DE26A8679F04 CRC64;
     MALLQISEPG MSAAPHRHRL AAGIDLGTTN SLVATVRSGS AACLPDADGR VTLPSVVRYL
     ENGGIEVGKT ALSAQKTDPL NTVSSAKRLI GRTLADLHQN THYLPYRFGD NQRFIELHTR
     QGVKTPVEVS AEILKTLKLR AEETLGGDLV GVVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA IAYGLDNASE GTFVVYDLGG GTFDVSVLQL TKGLFEVKAT GGNSALGGDD
     FDHRLFCYLL EQNRLSQLNE QDSQLLLSLV RAAKEQLTTQ TEARIQATLS DGMAIDTSIS
     RAEFHNLTQH LVMKTLEPVK QALKDAGVGK NEVKGVVMVG GSTRMPHVQQ AVATFFGQTP
     LNNLNPDEVV ALGAAIQANV LAGNKADGEW LLLDVTPLSL GLETYGGLAE KIIPRNSTIP
     TARAQDFTTF KDGQTAMTIH VVQGERELVS DCRSLAKFTL RGIPPMAAGA ARIRVTFQID
     ADGLLSVSAQ EQSTGVQAQI EVKPSYGLDD DTITQMLKDS MGNAAEDMAA RARAEAVVEA
     ESLTDAVNAA LELDSDLLDA EEFAQIQRDI ADLQGRLKDG KAEDIRAAVA KLSRSTDNFA
     AKRMNRNIQR ALTGQSVDNI