ID K7RJ62_ACIA4 Unreviewed; 477 AA.
AC K7RJ62;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Thrombospondin type 3 repeat protein {ECO:0000313|EMBL:AFV87924.1};
GN OrderedLocusNames=PACID_00730 {ECO:0000313|EMBL:AFV87924.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV87924.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV87924.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
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; CP003493; AFV87924.1; -; Genomic_DNA.
DR AlphaFoldDB; K7RJ62; -.
DR STRING; 1171373.PACID_00730; -.
DR KEGG; pbo:PACID_00730; -.
DR PATRIC; fig|1171373.8.peg.70; -.
DR eggNOG; COG2755; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_031283_0_0_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00146; PKD; 1.
DR CDD; cd01823; SEST_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR037460; SEST-like.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR37981; LIPASE 2; 1.
DR PANTHER; PTHR37981:SF1; SGNH_HYDRO DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637460-2}.
FT DOMAIN 328..414
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT REGION 412..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 119..130
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
SQ SEQUENCE 477 AA; 50614 MW; CC2055CBFC3509F9 CRC64;
MVRVALLGDS YSAGNGIRAG GYTFPGGYKG HGEYGSYQSD RNYASVLTKT LNSQVQGSTY
QLTMLAHSGA LLHNDPDDTN DKTVPEIGTQ VGRMDPRTGL VLVTAGGNDL KFSTVVKTCI
VLAYLSSGRC RQILDGDGST KYPSLDDRLA GVRASTQALL ARIQSRVTNP EQARVVLVGY
PYLADADLHV FADYGVGPQL RAAQDRFTAM QKDLVASWNA GHTLQVVFVD TSTVFLSHET
SSVLGNRNPK RWINEVLETA GDDYGLPGAT TTSMASLDMN NWYHPKIIGH RQMAVRIYSS
GAVKRSRAVI PGVDWSGLAS VPEPPRVAAD VMGSNIVKAG QQLSLDASSS FALEGRVTRY
EWDLDGDGSY ETSGSAPTVS VTYPSVRDVD VGLRVTTSTG LSATTVWGVS VTRDGDEVPD
GQDNCPADPN PGQDDFDGDG IGDVCGPDPG WTLRGQDATT SEGSASGKAG GDDASRR
//
