ID K0KL69_WICCF Unreviewed; 613 AA.
AC K0KL69;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE AltName: Full=Hsp70 chaperone Ssb {ECO:0000256|ARBA:ARBA00042875};
GN Name=SSB1 {ECO:0000313|EMBL:CCH41843.1};
GN ORFNames=BN7_1382 {ECO:0000313|EMBL:CCH41843.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH41843.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH41843.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70
CC subfamily. {ECO:0000256|ARBA:ARBA00037959}.
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:CCH41843.1}.
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DR EMBL; CAIF01000029; CCH41843.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KL69; -.
DR STRING; 1206466.K0KL69; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; K0KL69; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 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|RuleBase:RU003322};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Stress response {ECO:0000313|EMBL:CCH41843.1}.
SQ SEQUENCE 613 AA; 66014 MW; 8DF18416B8B87073 CRC64;
MAEGVFAGAI GIDLGTTYSC VATYDNAVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ
AALNPKNTVF DAKRLIGRRY DDESVQKDIK SWPFKIVDSN GAPLIEVDYL GEQKTFSPQE
ISSMVLTKMK EIAEAKIGQK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA
AAIAYGLGAG KSDKERHVLI FDLGGGTFDV SLLHIAGGVF TVKATAGDTH LGGQDFDTNL
LEHFKAEFKK KTGNDISGDA RALRRLRTAA ERAKRTLSSV ATTTVEVDSL FDGEDFASNI
SRARFEDINA ALFKSTLDPV EQVLKDAKIS KDAVDEVVLV GGSTRIPKVQ KLLSDFFNGK
QLEKSINPDE AVAYGAAVQG AILTGQSTSD DTKDLLLLDV SPLSLGVAMQ GNVFAPVVPR
NTTVPTIKRR TFTTVADHQT TVQFPVYQGE RVNCTENTLL GEFDLKGIPP LPAGEPVLEA
IFEVDANGIL KVTAVEKSTG KSANITISNA VGRLSTADIE KAIEEAEKFK SSDEAFSKRH
EAKQRLESYV SSIESTVTDP VLSSKLKRGS KDKIEAALSD ALAALEIEES SAEDYRKAEV
GLKRVVTKAM STR
//
