ID S6SQZ1_PSESF Unreviewed; 173 AA.
AC S6SQZ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000256|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000256|HAMAP-Rule:MF_00682,
GN ECO:0000313|EMBL:EPN33682.1};
GN ORFNames=A244_36255 {ECO:0000313|EMBL:EPN33682.1};
OS Pseudomonas syringae pv. actinidiae ICMP 18807.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=1194404 {ECO:0000313|EMBL:EPN33682.1, ECO:0000313|Proteomes:UP000015729};
RN [1] {ECO:0000313|EMBL:EPN33682.1, ECO:0000313|Proteomes:UP000015729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 18807 {ECO:0000313|EMBL:EPN33682.1,
RC ECO:0000313|Proteomes:UP000015729};
RX PubMed=23935484; DOI=10.1371/journal.ppat.1003503;
RA McCann H.C., Rikkerink E.H., Bertels F., Fiers M., Lu A., Rees-George J.,
RA Andersen M.T., Gleave A.P., Haubold B., Wohlers M.W., Guttman D.S.,
RA Wang P.W., Straub C., Vanneste J.L., Rainey P.B., Templeton M.D.;
RT "Genomic analysis of the Kiwifruit pathogen Pseudomonas syringae pv.
RT actinidiae provides insight into the origins of an emergent plant
RT disease.";
RL PLoS Pathog. 9:E1003503-E1003503(2013).
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, ECO:0000256|HAMAP-
CC Rule:MF_00682}.
CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC {ECO:0000256|HAMAP-Rule:MF_00682}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000256|ARBA:ARBA00010476,
CC ECO:0000256|HAMAP-Rule:MF_00682}.
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:EPN33682.1}.
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DR EMBL; AOKG01002488; EPN33682.1; -; Genomic_DNA.
DR RefSeq; WP_005615768.1; NZ_ANJL01000001.1.
DR AlphaFoldDB; S6SQZ1; -.
DR GeneID; 61790082; -.
DR PATRIC; fig|1194404.4.peg.7446; -.
DR Proteomes; UP000015729; Unassembled WGS sequence.
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 GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00682; HscB; 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; PF00226; DnaJ; 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, ECO:0000256|HAMAP-Rule:MF_00682}.
FT DOMAIN 5..77
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 173 AA; 20210 MW; 95FD958671FF4A2C CRC64;
MGSPCHFALF ELKPEFQLDL DQLATRYREL ARNVHPDRFA DASEREQRLA LERSASLNEA
YQTLKSPPKR ARYLLAMNGN EVPLEVTVHD PEFLLQQMQL REDLEDLQDE ADLAGVATFK
RQLKVAQDEL NQSFAACWND AAQREHAEKL MRRMQFLDKL SHEVRQLEER LDD
//
