ID F9ZG33_9PROT Unreviewed; 471 AA.
AC F9ZG33;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:ADZ25935.1};
DE EC=3.4.21.108 {ECO:0000313|EMBL:ADZ25935.1};
DE Flags: Precursor;
GN ORFNames=NAL212_1018 {ECO:0000313|EMBL:ADZ25935.1};
OS Nitrosomonas sp. AL212.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25935.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ25935.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ25935.1,
RC ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP002552; ADZ25935.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZG33; -.
DR STRING; 153948.NAL212_1018; -.
DR KEGG; nit:NAL212_1018; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_4; -.
DR Proteomes; UP000001629; Chromosome.
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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADZ25935.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ADZ25935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001629};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039350234"
FT DOMAIN 363..455
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 352..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 50874 MW; 663636BA7F8C35B4 CRC64;
MFQLIIIPFI LLSSVTFVQA TELPDFTGLV EKHGVAVVNI SAVQSLNVMS NQIIPEIPGI
PENSPFYDFF RRHIQPFPGP RKSEPKSLGS GFIISSDGYI LTNAHVVETA DEITVKLNDK
REFVAEIIGT DRKTDIALIK ISATDLPVVT QGNPENLKVG EWVIAIGSPF GFEHSVTAGI
VSAKGRSLAQ ENYVPFIQTD VAINPGNSGG PLFNMKGEVV GINSQIYSRT GGFMGLSFAI
PINVATEIAD QLKTSGKVSR GRIGVMIQEV TKELAESFGL TDSRGALVVS IEKDGPAGKA
GVQARDIILK FDEKEVLTSS DLPRIVGNTK PGSKATIQIW RDGALRTIKV EVGETPSDEG
AESRKLKQSK KPDTSNRLGL ALSEVTDEQK KQLEIANGLL VEDMQSGIAS RSGIRIGDII
LGFNSKDVKS VAQFNELLNQ VKSGKNIALL VKRGDITTFI TMKLSDDEKE N
//
