ID N9KT09_ACIBA Unreviewed; 172 AA.
AC N9KT09;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-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 ORFNames=F913_02483 {ECO:0000313|EMBL:ENW71600.1};
OS Acinetobacter baumannii NIPH 80.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=1217629 {ECO:0000313|EMBL:ENW71600.1, ECO:0000313|Proteomes:UP000013021};
RN [1] {ECO:0000313|EMBL:ENW71600.1, ECO:0000313|Proteomes:UP000013021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 80 {ECO:0000313|EMBL:ENW71600.1,
RC ECO:0000313|Proteomes:UP000013021};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter baumannii NIPH 80.";
RL Submitted (FEB-2013) 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, 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:ENW71600.1}.
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DR EMBL; APRE01000048; ENW71600.1; -; Genomic_DNA.
DR RefSeq; WP_001015254.1; NZ_KB849947.1.
DR AlphaFoldDB; N9KT09; -.
DR SMR; N9KT09; -.
DR GeneID; 66397312; -.
DR PATRIC; fig|1217629.3.peg.2406; -.
DR HOGENOM; CLU_068529_2_0_6; -.
DR Proteomes; UP000013021; 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 2..69
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 172 AA; 20136 MW; B7CD5320029CF3CA CRC64;
MNHFELFNLP VALDIDLASL KSNFLSLQQQ YHPDKAADKD QALIKSSEIN QAFKTLSQVD
SRAAYLLALK KQDHHLDQSI SDFEFLQSAL ELREQLDEAT SSEHLRTLRL EVQQWIDGLV
REFKIDYSEE DWAEARDTVR KLRFFQRVLN DIDKAEDQLL DDEDSFDLDD DF
//
