ID A0A1F8P5L1_9CHLR Unreviewed; 868 AA.
AC A0A1F8P5L1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=A2Z15_02820 {ECO:0000313|EMBL:OGO18454.1};
OS Chloroflexi bacterium RBG_16_50_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797642 {ECO:0000313|EMBL:OGO18454.1, ECO:0000313|Proteomes:UP000179337};
RN [1] {ECO:0000313|EMBL:OGO18454.1, ECO:0000313|Proteomes:UP000179337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the TolB family.
CC {ECO:0000256|ARBA:ARBA00009820}.
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:OGO18454.1}.
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DR EMBL; MGNJ01000089; OGO18454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8P5L1; -.
DR Proteomes; UP000179337; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032485; LRP1-like_beta_prop.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF16472; DUF5050; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
FT DOMAIN 54..97
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 868 AA; 91939 MW; 86623EC78539EC82 CRC64;
MKRALFTAGM AFLLLSVILA FIGCGGLPDV KFNKSVNGGP APLNVAFTNT TEVSGDDTST
VFKWDFGDGK TLETSNAKEP VSHEYTKTGT YTITLSIYKK DSPENKKTLS QNVTVTHGAV
DSVKITPQTV TLNIGQSQTF KSEVLDIYGN LISTAVLVWK AEAGAITDTG TLVAGTTAGT
FTPGVTVDAS LDSYSAHSSA SVTVNPDPLA TASLPAVEIA AGGTIQLEVV AEDKYGNVIE
NLETTWKLLN TEAGAITDKG LFTAQKKAGS FEQAIEVQVK QGDKVLQAKG KVTIVPAALS
QIGIAPGKID LGMGMTQQYV AVGADKYGNR ISGVSFTWSA ISSAGTMTAK GLFTAGNNPG
TYKDGIIVTA TKESLAIIKT TDVIVNPDRI LFFSNRADET STNLDIYIMD IDGSNVQRVI
TSQGTQDLNI SCSPDGRRFV FAEIFDSGST VYLANVDGSQ QISIVTGKRY YEPNWSHDGQ
KIAFQSWEDD DGEIFIMDID GGNMVRLTDN TLYDDFPDWS PNGSKIVYVS QPNSSTDAKI
YVMNTDGSGK QQLTTGSGYD ILPQWSPDST QIAFQTSRGA LITYSVFVMN ADGSNLRAIS
SSSAFNSDGP SWSPDGTKIA FLNFTSANQG EIYTVNVDGT NLTRLTNNTA RDMWPKWLPR
AQGVKVTEAS AVIATSFDVP SMTAQQITAM ASPAVVRIKT NLGSGTGFII GSSGLIMTNN
HVISDATEIT VYLTDGTSYA GTVQSRDMVR DLAIVKIQAT GLPTLEIASL DGVSAGQQVY
VLGYPLGQEN VSVTSGLLSS IEFDDGRNVT WLQTDSAVNP GNSGGPLLDS QGRVIGVVAA
KMVGVSVEGI GFAISANTVN TYLSELLD
//
