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Database: UniProt
Entry: A0A0F7KBA1_9PROT
LinkDB: A0A0F7KBA1_9PROT
Original site: A0A0F7KBA1_9PROT 
ID   A0A0F7KBA1_9PROT        Unreviewed;       477 AA.
AC   A0A0F7KBA1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:TYP80561.1};
DE   SubName: Full=Peptidase S41 {ECO:0000313|EMBL:AKH37690.1};
GN   ORFNames=AAW31_07530 {ECO:0000313|EMBL:AKH37690.1}, BCL69_105816
GN   {ECO:0000313|EMBL:TYP80561.1};
OS   Nitrosomonas communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37690.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH37690.1, ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH37690.1,
RC   ECO:0000313|Proteomes:UP000034156};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT   Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [3] {ECO:0000313|EMBL:TYP80561.1, ECO:0000313|Proteomes:UP000324176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:TYP80561.1,
RC   ECO:0000313|Proteomes:UP000324176};
RA   Wagner M.;
RT   "Active sludge and wastewater microbial communities from Klosterneuburg,
RT   Austria.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CP011451; AKH37690.1; -; Genomic_DNA.
DR   EMBL; VNHT01000058; TYP80561.1; -; Genomic_DNA.
DR   RefSeq; WP_046849765.1; NZ_VNHT01000058.1.
DR   AlphaFoldDB; A0A0F7KBA1; -.
DR   KEGG; nco:AAW31_07530; -.
DR   PATRIC; fig|44574.3.peg.1827; -.
DR   OrthoDB; 9812068at2; -.
DR   Proteomes; UP000034156; Chromosome.
DR   Proteomes; UP000324176; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00988; PDZ_CTP_protease; 1.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.750.44; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   NCBIfam; TIGR00225; prc; 1.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004404};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:TYP80561.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034156};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..477
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033222220"
FT   DOMAIN          92..160
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          413..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  51692 MW;  B5C8414C279757E6 CRC64;
     MHNFIKKLSL ILSGVAAGVM ISLNFSAVAD KALKAELPPL PIEELRAFTQ VFGRIKSDYV
     EPVDDKKLIT EAINGMLVGL DPHSAYLDSE EYKELQIGTQ GEFGGLGIQV TMEDGLVKVI
     SPIEDTPAFR AGIKTGDLII KLDDTAVKGM TLNEAIKLMR GKPNTSITLT IAREGEGEPL
     EFTLMRAIIK IESVKAKLVE PGYGYLRVTQ FQEQTGENLA QAIEKLFKES KTPMKGLVLD
     LRNDPGGLLN SAVAVSAAFL PANALIVYTE GRTSDAKMRL MANPEYYLRG PGKDFIAGLP
     SEIKTVPMVT LVNGGSASAS EIVAGALQDH KRSIVMGTQT FGKGSVQTIL PLGNNTAIKL
     TTARYYTPNG QSIQAKGITP DIIDETDDAS RQLRESDLSR HLRSNKVDEV LKIDATDSQK
     ANESDDKPKS KKSSSKRKTP LEFGSNDDLL LTKAIKHLKG MDADAKRKST KTAKKSS
//
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