ID A0A099KME9_9GAMM Unreviewed; 207 AA.
AC A0A099KME9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein TorD {ECO:0000256|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000256|HAMAP-Rule:MF_01150};
GN ORFNames=ND16A_0158 {ECO:0000313|EMBL:KGJ91082.1};
OS Thalassotalea sp. ND16A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ91082.1, ECO:0000313|Proteomes:UP000029848};
RN [1] {ECO:0000313|EMBL:KGJ91082.1, ECO:0000313|Proteomes:UP000029848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND16A {ECO:0000313|EMBL:KGJ91082.1,
RC ECO:0000313|Proteomes:UP000029848};
RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA Hazen T.C.;
RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT Eastern Mediterranean Deep Water.";
RL Submitted (AUG-2014) 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 -!- 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:KGJ91082.1}.
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; JQDZ01000097; KGJ91082.1; -; Genomic_DNA.
DR RefSeq; WP_033078419.1; NZ_JQDZ01000097.1.
DR AlphaFoldDB; A0A099KME9; -.
DR STRING; 1535422.ND16A_0158; -.
DR PATRIC; fig|1535422.3.peg.2868; -.
DR eggNOG; COG3381; Bacteria.
DR OrthoDB; 7849731at2; -.
DR Proteomes; UP000029848; Unassembled WGS sequence.
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:UP000029848}.
SQ SEQUENCE 207 AA; 23475 MW; 3163564D5AD65194 CRC64;
MNSINSARAM FYGLLSSLFA KEVERDLLSE LMSEQGQVFL QHLANEDSFQ PHIGVLNDKL
KSLSSERDLL ELAADFCGLF LVSGKHSASP YAGQYLEKDS AELFGEYHQS MVNFLTEHEM
QLHSDFPEPA DHIAVIFAYL SYLCSNASRA EQLSFIDNYL LTWVESFAQQ VQQHDQQGFY
SALASLSRAW LEFDRENLVN ENADNAE
//
