ID V9H7E4_9NEIS Unreviewed; 619 AA.
AC V9H7E4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=HMPREF9021_02206 {ECO:0000313|EMBL:EFG29945.1};
OS Simonsiella muelleri ATCC 29453.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Simonsiella.
OX NCBI_TaxID=641147 {ECO:0000313|EMBL:EFG29945.1, ECO:0000313|Proteomes:UP000017813};
RN [1] {ECO:0000313|EMBL:EFG29945.1, ECO:0000313|Proteomes:UP000017813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG29945.1,
RC ECO:0000313|Proteomes:UP000017813};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F., Haas B.,
RA Nusbaum C., Birren B.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFG29945.1, ECO:0000313|Proteomes:UP000017813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG29945.1,
RC ECO:0000313|Proteomes:UP000017813};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Simonsiella muelleri ATCC 29453.";
RL Submitted (OCT-2011) 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:0000256|HAMAP-Rule:MF_00679}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679,
CC ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFG29945.1}.
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DR EMBL; ADCY02000063; EFG29945.1; -; Genomic_DNA.
DR RefSeq; WP_002643019.1; NZ_JH815313.1.
DR AlphaFoldDB; V9H7E4; -.
DR STRING; 641147.HMPREF9021_02206; -.
DR KEGG; smur:BWP33_06240; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000017813; Unassembled WGS sequence.
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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Reference proteome {ECO:0000313|Proteomes:UP000017813}.
SQ SEQUENCE 619 AA; 66684 MW; 977EF021D09AAEED CRC64;
MALLQIAEPN MSATPHQHRL TVGIDLGTTN SLVATVKSGT ATCLPDELGN VSLPSVVRYL
GDDKLIVGKK ALAQQKLDPQ NTISSAKRLI GRTLPEIDTT HLPYRFGKSE KIIELQTKNG
AKTPIDVSAD ILRTLRERAE QSLGGELVGA VITVPAYFDD AQRQATKDAA RLAGLNVLRL
LNEPTAAAIA YGLDNGAEGT FVVYDLGGGT FDVSVLELSK GLFQVKATGG NSALGGDDFD
HRLFCHIIEN NQLSLTNEHD IQLLFSLVRQ AKETLSKQPE TRIQATLNNG TEINTLITRA
EFHALTQHLI AKTIEPVKQA LKDAGVSKSD IKGVIMVGGA TRMLHVQQAV GAFFGQTPLN
NLNPDQVVAL GAAMQANVLA GNKNDDEWLL LDVTPLSLGL ETYGGLVEKI IPRNSTLPTA
RAQDFTTFKD GQTAMTIHVV QGERELVADC RSLAKFTLRG IPPMVAGAAR IRVTFQVDAD
GLLSVSAREQ TTGVQAQIEV KPSYGLDDET ITQMLRDSMN NAKDDAAARA RAEAKVEAES
LIGAIQAALD LDADLLSEEE LNKINQLMTK LASNLETESA ENIRTAVHEL SHETDDFAAR
RMDRNIQRVL GGVNVADLS
//
