ID H3ZCN9_9ALTE Unreviewed; 618 AA.
AC H3ZCN9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679,
GN ECO:0000313|EMBL:EHR41619.1};
GN ORFNames=AJE_05561 {ECO:0000313|EMBL:EHR41619.1};
OS Alishewanella jeotgali KCTC 22429.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR41619.1, ECO:0000313|Proteomes:UP000012046};
RN [1] {ECO:0000313|EMBL:EHR41619.1, ECO:0000313|Proteomes:UP000012046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR41619.1,
RC ECO:0000313|Proteomes:UP000012046};
RX PubMed=22461542; DOI=10.1128/JB.00153-12;
RA Jung J., Chun J., Park W.;
RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella jeotgali
RT Isolated from Traditional Korean Fermented Seafood.";
RL J. Bacteriol. 194:2097-2097(2012).
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:EHR41619.1}.
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DR EMBL; AHTH01000011; EHR41619.1; -; Genomic_DNA.
DR RefSeq; WP_008950044.1; NZ_AHTH01000011.1.
DR AlphaFoldDB; H3ZCN9; -.
DR STRING; 1129374.AJE_05561; -.
DR PATRIC; fig|1129374.4.peg.1113; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000012046; 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:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}.
SQ SEQUENCE 618 AA; 65767 MW; A143714B5CD17AD3 CRC64;
MALLQIAEPG QSAAPHQHKL AAGIDLGTTN SLVATVRSGE AKVLLNQAGE AMVPSVVRYG
AEQVVVGSAA VAAAVSDPEN TIVSVKRLMG KGYQETLALT EKLPYQLIEQ SGLVAIETAA
GVKNPVEVSA EILATLANTA SQTLGGELNG VVITVPAYFD DAQRQATKDA AKLAGLNVLR
LLNEPTAAAL AYGLDSGQEG IIAVYDLGGG TFDISILRLR RGVFEVLATG GDSALGGDDF
DQALVALLQQ QHDQPNLSAS ARRQYQQQAK AIKERLTNSD STDYSFSADG QQLSGSVSRQ
QFEDLISPLV KQTIRACRQS LRDAGLTADE VLKVVLVGGS TRVPLVRQQV TSFFGSEPLT
SIDPDQVVAI GAAIQANVLV GNKADNETLL LDVIPLSLGI ETMGGLTEKI IPRNTVIPVA
RAQEFTTFKD GQTAMAIHVV QGERELVEDC RSLARFELRG IPPMPAGGAH IRVTFQVDAD
GLLSVSAMEK STGVQASIQV KPSYGLTDDQ VAQMISGSMQ YARQDMQQRL LREQQVEAER
VLEAVSAALA TDAALLNEHE LATIRDALRQ LAELKQQGDT AAIKAAIEHT NQLTDDFAAR
RMDKSIRLAL QGHKVDEV
//
