ID G0AAC4_COLFT Unreviewed; 507 AA.
AC G0AAC4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative periplasmic serine protease {ECO:0000313|EMBL:AEK63138.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:AEK63138.1};
GN OrderedLocusNames=CFU_3314 {ECO:0000313|EMBL:AEK63138.1};
OS Collimonas fungivorans (strain Ter331).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392};
RN [1] {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63138.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT expression of ribosomal RNA genes by large-insert library fluorescent in
RT situ hybridization (LIL-FISH).";
RL Environ. Microbiol. 6:990-998(2004).
RN [2] {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63138.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT "Genomic flank-sequencing of plasposon insertion sites for rapid
RT identification of functional genes.";
RL J. Microbiol. Methods 66:276-285(2006).
RN [3] {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63138.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA Leveau J.H.;
RT "Identification and characterization of genes underlying chitinolysis in
RT Collimonas fungivorans Ter331.";
RL FEMS Microbiol. Ecol. 66:123-135(2008).
RN [4] {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63138.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA Leveau J.H., Uroz S., de Boer W.;
RT "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT solutions to life in oligotrophic soil environments.";
RL Environ. Microbiol. 12:281-292(2010).
RN [5] {ECO:0000313|EMBL:AEK63138.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63138.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA van den Berg M., Leveau J.H.;
RT "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT Collimonas fungivorans versus Aspergillus niger.";
RL ISME J. 5:1494-1504(2011).
RN [6] {ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA Leveau J.H.;
RT "Complete sequence of Collimonas fungivorans Ter331.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP002745; AEK63138.1; -; Genomic_DNA.
DR AlphaFoldDB; G0AAC4; -.
DR STRING; 1005048.CFU_3314; -.
DR KEGG; cfu:CFU_3314; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_4; -.
DR Proteomes; UP000008392; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEK63138.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AEK63138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008392};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..393
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 407..497
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 507 AA; 52778 MW; A1588671BED0ABF3 CRC64;
MLCASSNPSA KEHSMSRQTR QTFIRSAIAI AVLVVAGGTY LHSKNGDIGI DNANAAIVAP
APVVSNTAPA VAVATDFSGI VERAGPAVVN ISVTGKAKQS AVSDQDDELD PNDPFSQFFK
RFGPQLQIPR HPQIMRGEGS GFIISADGLI LTNAHVVEGA SEVTVKLTDR REFRAKVLGS
DKQSDIAVIR IDAKNLPIVQ IGNPALTRVG EPVLAIGSPY GFENTATAGI VSAKSRSLPD
DTYVPFIQTD VAVNPGNSGG PLFNIKGEVI GINSQIYSQT GGYQGLSFAI PIDVATKVEQ
QLVKHGKVTR SHLGVSVQEV NQALAESFGL KSAAGALVSS VDKGSPADKG GLQTGDVILR
FNGQPISHSS DLPSLVADTA PGTASTIEVV RNGQPKTLTV KPTEAEAVKT ASNDEGAGSQ
ARLGLALRQL SPDEQQQVGI HGGLVVEDAS GPSALAGIQR GDVILSLNGK PVNSVEQLRQ
LVSKAGKNVA LLVQRDKDKI FVPLNLG
//
