ID I4W0D9_9GAMM Unreviewed; 390 AA.
AC I4W0D9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:EIL92930.1};
GN ORFNames=UU7_10147 {ECO:0000313|EMBL:EIL92930.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL92930.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL92930.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL92930.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EIL92930.1}.
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DR EMBL; AJXT01000028; EIL92930.1; -; Genomic_DNA.
DR RefSeq; WP_007807967.1; NZ_AJXT01000028.1.
DR AlphaFoldDB; I4W0D9; -.
DR STRING; 1163407.UU7_10147; -.
DR PATRIC; fig|1163407.3.peg.2044; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000003226; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EIL92930.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..354
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 390 AA; 40215 MW; 539457A0D7B2AAED CRC64;
MKHAAGTLLF IARFAILGLA MAFVVGLFWP GSGERLRARF GLTESVHAPA ASQPRVGNGP
VSYADAVAAA APSVVNIYAN KIVTEQAVRM YDNPVLQQLF GGQPTTYQHR EQTLGSGVIV
NAQGYVLTNN HVIAHAADIQ VLLYDGRIAQ ARLVGADEES DLAVLKIDAS NPPVIPIASE
DPRPGDVVLA IGNPLGLNQT VTMGIVSAIG RQLNSSSAED FIQTDAAINL GNSGGALVNA
EGQLVGINTL LIGKAAGAEG IGFAIPVTTA KKVLDQIIAT GHVVRGWLGA DYAFVPVAAN
SGLPAAARGA LVTNVYPGSP AALAGIKPRD ILLRIGSEDI LDPASLRRSE AALKPGSKVE
ISGLRNGSPF HAEATVAQRP AMGTNALSGD
//