ID F8GKJ4_NITSI Unreviewed; 471 AA.
AC F8GKJ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:AEJ01758.1};
GN OrderedLocusNames=Nit79A3_1960 {ECO:0000313|EMBL:AEJ01758.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01758.1};
RN [1] {ECO:0000313|EMBL:AEJ01758.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01758.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP002876; AEJ01758.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GKJ4; -.
DR STRING; 261292.Nit79A3_1960; -.
DR KEGG; nii:Nit79A3_1960; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_4; -.
DR OMA; PIVMSAD; -.
DR OrthoDB; 9758917at2; -.
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; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AEJ01758.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039615752"
FT DOMAIN 363..455
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 105
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 471 AA; 50787 MW; 7F6CE7E573E04604 CRC64;
MLQLILISLF FYSSTVLAQA NELPDFTGLV EKHGAAVVNI SAVQNLTTLN NQIVPEIPGI
PENSPFYDFF KRHMQPFPAP RKSEPKSLGS GFIISSDGYI LTNAHVVETA DEITVKLNDK
REFVAEIIGT DRKTDIALIK INATDLPKVT QGNPENLKVG EWVVAIGSPF GFEHSVTAGI
VSAKGRSLAQ ENFVPFIQTD VAINPGNSGG PLFNMKGEVV GINSQIYSRT GGFMGLSFAI
PINVATEIAD QLKVSGKVSR GRIGVMIQEV TKELAESFGL TDGKGALVVS VEKGGPADLA
GIKARDIIVQ FDEKGITTSA DLPRIVGNTK PGTKVSIQIW RDGSLKTVKV EVGETPSDEA
AENRKLKQGK KTDTSNRLGL ALSEITAEQK KQLEISNGLL VEDMQPGIAS RSGIRIGDII
LGFNSKDVNS IEQFNELLKQ VKSGKNIALL VKRGDITTFI TMKLTDDDKK N
//