ID H1YCK0_9SPHI Unreviewed; 176 AA.
AC H1YCK0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Co-chaperone Hsc20 {ECO:0000313|EMBL:EHQ30678.1};
GN ORFNames=Mucpa_6627 {ECO:0000313|EMBL:EHQ30678.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ30678.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ30678.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ30678.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Co-chaperone involved in the maturation of iron-sulfur
CC cluster-containing proteins. Seems to help targeting proteins to be
CC folded toward HscA. {ECO:0000256|ARBA:ARBA00025596}.
CC -!- SIMILARITY: Belongs to the HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001403; EHQ30678.1; -; Genomic_DNA.
DR RefSeq; WP_008512601.1; NZ_CM001403.1.
DR AlphaFoldDB; H1YCK0; -.
DR STRING; 714943.Mucpa_6627; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_068529_2_0_10; -.
DR OrthoDB; 287587at2; -.
DR Proteomes; UP000002774; Chromosome.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774}.
FT DOMAIN 4..78
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 176 AA; 20432 MW; 3708BE9178F611A3 CRC64;
MTTSYFEFYG LPESFTIDAK VLKNKFYELS KRYHPDFYAN ESEARQQEIL ELSTLNNKAY
QVLSNPPKLT EYILQQHGLL AEGDKHQLAP DFLMEMMEIN ENLMEVDDEA GLLAIKTQLA
GIENDLNAQL SSLIKNYETD NQANKITTLK NIKDIYFKQK YLLRIKDSLN TFAARF
//
