ID A0A0C5WBE3_9GAMM Unreviewed; 217 AA.
AC A0A0C5WBE3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Chaperone protein TorD {ECO:0000256|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000256|HAMAP-Rule:MF_01150};
GN ORFNames=H744_2c2273 {ECO:0000313|EMBL:AJR08936.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR08936.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR08936.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR08936.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before the
CC insertion of the molybdenum cofactor and, as a result, probably favors
CC a conformation of the apoenzyme that is competent for acquiring the
CC cofactor. {ECO:0000256|HAMAP-Rule:MF_01150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01150}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01150}.
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; CP005974; AJR08936.1; -; Genomic_DNA.
DR RefSeq; WP_044623532.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WBE3; -.
DR STRING; 658445.H744_2c2273; -.
DR KEGG; pgb:H744_2c2273; -.
DR PATRIC; fig|658445.3.peg.4266; -.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OrthoDB; 7849731at2; -.
DR Proteomes; UP000032303; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1820; -; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR HAMAP; MF_01150; TorD; 1.
DR InterPro; IPR023069; Chaperone_TorD.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR036411; TorD-like_sf.
DR PANTHER; PTHR34227:SF11; CHAPERONE PROTEIN TORD; 1.
DR PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR SUPFAM; SSF89155; TorD-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01150};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01150};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303}.
SQ SEQUENCE 217 AA; 24653 MW; D4D9586F7F0C555A CRC64;
MKEFIAFNEQ RAEIYWWMSS LFARELTEQD IEQYRGGEMV TFLSGLAMTP ELKQPVEAFR
AALNRLESRE DAQLELAADF CGLFLSTPKS GALPYASMYV GESGLMNDKP AQDMNKLMEE
YGIAQRKEFN EPADHLAVEL DFMGNLIIMA NQQDSEEQAE PMMQAQLDFI NTMLLNWLPA
FAAEVKQRDP FGFYAAAAEV LTAFCHLDVT FLKGEEQ
//
