ID   A0A077LY22_9MICO        Unreviewed;      1124 AA.
AC   A0A077LY22;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN12_350004 {ECO:0000313|EMBL:CCH78798.1};
OS   Tetrasphaera japonica T1-X7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH78798.1, ECO:0000313|Proteomes:UP000035721};
RN   [1] {ECO:0000313|EMBL:CCH78798.1, ECO:0000313|Proteomes:UP000035721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T1-X7 {ECO:0000313|EMBL:CCH78798.1,
RC   ECO:0000313|Proteomes:UP000035721};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH78798.1}.
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DR   EMBL; CAJB01000279; CCH78798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077LY22; -.
DR   STRING; 1194083.BN12_350004; -.
DR   Proteomes; UP000035721; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   InterPro; IPR032109; Big_3_5.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   Pfam; PF16640; Big_3_5; 5.
DR   Pfam; PF18911; PKD_4; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 2.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035721};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1124
FT                   /note="PKD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001720828"
FT   TRANSMEM        1093..1113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..204
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          293..477
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          979..1039
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          396..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1036..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1124 AA;  110479 MW;  536B795E1FDC1455 CRC64;
     MPAVIALVVG WLVAVTPAAS ADGPTTFSNS TSIAIPATGS TDQMGPASPY PSTIAVSGLS
     GSVTKVTVTF GGLTHSTVND IDAMVVAPSG ENLIVMSDVG DPSTLAFAND VNLTFDDAAA
     GPVPTGNIPS GSYRPTNNVN ADGTSTDTFP TPAPTPSNET TLAGAFTGID PNGTWRLYVV
     DDGSGDTGTM TDGWSLTVTT ETAAVATTTT VATSHTPSTT GDPVTFTATV RAGGTPVTSG
     SVRFVDGTTS LGAPVDLGGS GTASITTSDL TEGTHEIRAT YSGATGFLTS NGTVSQRVDN
     ATVADGDTFC NTGPITVPSV GAAQPYPSHI TVSGQAGTVT KVTATLKGLS HQAPIDLDVM
     LSGPDPSRNL LLLSDTGGQN PVSDLTVGFD DDAAGAVPVP LTSGTFRPTD DDEDGGSDTF
     PAPAPASSGA TTLSTFDGSS ADGQWSLWVN DDATGDSGSI ADGWCLTVTS QVATQTTVTA
     DPNPSTSGSS VTFTATVNAG SDPVTSGTVQ FRDGAADLGT PVAVGADGTA TFTTSDLTVG
     SHAITAAYGG FGTFAASSGS VTQVVEKTAT TTTLTSTLNP STVGQPVTFT ADVTAGGDPV
     TTGTVTFSVD GVDGAPTALG GDGTATLLVP TFDAGTHTAV AHYDGSATLA TSDDSLDQVV
     DLVDTATTLT TDPNPSTVGQ SVTLTATVTA GGDPVTSGTV EFFDGATSLG SAPVVSGSAS
     FTTTSPLAVG SHTLTARYSG TSTYAESSGG AEQVVEGLAT VTTLTSSDNP SAAGDPVDIT
     ATVTAGGSPV DAGTVVFTVD GVDRPPVTVA SDGTATTTLA APTPGMHSVL AAYSGTDIYL
     SSEDSLDQGV APEANAGGAY AVAEGGTLSL DASGSTTGAT VAWDLNDDGD FTDATGVSPT
     VTWDQLEALG IDDGPSTRTV RARITLGSLT STATTSLTVT NTPPTATVTG DLMATAGQPF
     TVKVGAEDPS SADLAASFTY TVDWGDGSPV ETVTGPADPP VTHTYATAGD YSASFVAQDK
     DGGTGEPTSV TVTAAAATTT STSSTTSTST SSSTTSSTGT SSTGPTSTTE PSLPSSTSSG
     SGGSLAFTGT DTLGPLLVAA VFVLAGALAL GLARRRRGST GRHD
//