ID R5EDL0_9BURK Unreviewed; 619 AA.
AC R5EDL0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=BN548_01383 {ECO:0000313|EMBL:CCX86151.1};
OS Parasutterella excrementihominis CAG:233.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=1263099 {ECO:0000313|EMBL:CCX86151.1, ECO:0000313|Proteomes:UP000018034};
RN [1] {ECO:0000313|EMBL:CCX86151.1, ECO:0000313|Proteomes:UP000018034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:233 {ECO:0000313|Proteomes:UP000018034};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX86151.1}.
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DR EMBL; CAXE010000062; CCX86151.1; -; Genomic_DNA.
DR AlphaFoldDB; R5EDL0; -.
DR Proteomes; UP000018034; 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.
DR PROSITE; PS01036; HSP70_3; 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}.
SQ SEQUENCE 619 AA; 67145 MW; C686E48C2A28FD4E CRC64;
MSLLQIAEPG MSTAPHEERF AVGIDLGTTN SLAATVRNGS PEVLVDEKNQ KLLPSVVHYE
KNGCVVVGEE ARSRAEADPL NTISSVKRLM GRSASELQNN RYMPYDFIKG EGMVKLNTAQ
GAKSPVEVSA EILKVLKKRA EDALGGELVG AVVTVPAYFD DAQRQATKDA AKLAGLNVLR
LLSEPTAAAL AYGLDTGAEG LYIVYDLGGG TFDVSVLRLR KGVFEVLATG GNSQLGGDDF
DQRLYCWVID QAGRPLLTHS DSRMLMAKAK AAKETLTTEK KATIHAKISG DRIINVTITR
EVFDSITHHL VARTIEATKQ TLKDAGLKRD EVKGVVLVGG STRMPCIRKA VADYFDREPL
TDIDPDEVVA IGAALQANLL AGNRSDEDWL LLDVTPLSLG LETMGGLVEK VIPRNTPIPV
AMAQDFTTFK DGQTAMSIHV LQGERDLVEE CRSLAKFSLR GIPPKVAGAA RIRVTFQVDA
DGLLSVTARE QTTGVEASVT VKPSYGLSED EISRMLEDSF GHAEEDMKLR ELREQKVEAA
RLLESIYSAL SSDADLLNEA ERAQIDAMIQ HLETVRAQDD KDEIKNSISA LSEGTKDFAA
RRMNRTILEA LQGKSVDEV
//