ID I7IXV0_9CORY Unreviewed; 536 AA.
AC I7IXV0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Detergent sensitivity rescuer dtsR2 {ECO:0000313|EMBL:CCI84083.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:CCI84083.1};
GN Name=dts2 {ECO:0000313|EMBL:CCI84083.1};
GN ORFNames=BN46_1367 {ECO:0000313|EMBL:CCI84083.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:CCI84083.1, ECO:0000313|Proteomes:UP000011016};
RN [1] {ECO:0000313|EMBL:CCI84083.1, ECO:0000313|Proteomes:UP000011016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:CCI84083.1,
RC ECO:0000313|Proteomes:UP000011016};
RX PubMed=23045487; DOI=10.1128/JB.01412-12;
RA Brinkrolf K., Schneider J., Knecht M., Ruckert C., Tauch A.;
RT "Draft Genome Sequence of Turicella otitidis ATCC 51513, Isolated from
RT Middle Ear Fluid from a Child with Otitis Media.";
RL J. Bacteriol. 194:5968-5969(2012).
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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:CCI84083.1}.
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DR EMBL; CAJZ01000201; CCI84083.1; -; Genomic_DNA.
DR RefSeq; WP_004602003.1; NZ_JH815195.1.
DR AlphaFoldDB; I7IXV0; -.
DR OrthoDB; 4434131at2; -.
DR Proteomes; UP000011016; Unassembled WGS sequence.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:CCI84083.1}.
FT DOMAIN 17..273
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 282..518
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 57517 MW; 757526E94D6ED997 CRC64;
MTDDSSSSGA APAAPTTASR LEELKQRRAE AAAPMGEARL DKVRDAGRLP ARDRIDYLLD
EGSFVELDRD ARHRTHDFGM QTRRPLTDGI VTGYGTIDGR GVCVFSQDGT VFGGALGEVY
GEKMIKLMEL AQKTGRPLIG LYEGAGARVQ DGSVSLDLIA QTFFQNVQAS GVVPQISVIM
GSCAGGNAYS PALTDFVVMV NKTSKMFVTG PDVITTVTGE QITQEELGGA SIHMGSSGAS
HYTAQDDEDA LDWVKELVSY LPGNNRELPP REPAEPEDGI TAQDEELNSI IPDSASVPYD
VRDVISVIAD EDVYLEIQED RAANVVTAFA RVDGEVVGFV ANQPTELAGC LDIDSAEKAA
RFVRTCDAFN IPLVLLVDVP GFLPGVEQEK GGILRRGAKL LYAYAEATVP KITVTMRKAY
GGAYCAMGSK GLGADINLAW PTAEIAVMGA SGAVPFIHRR RIAAARDAGE DVDALVAELE
REYSEHMLSP YLAAERGLID EVILPEETRL RVAASLDLLR DKAEVRADRK HGNIPL
//
