ID   V9WML4_9PSED            Unreviewed;       664 AA.
AC   V9WML4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Peptidase M3 {ECO:0000313|EMBL:AHD12221.1};
GN   ORFNames=C163_00260 {ECO:0000313|EMBL:AHD12221.1};
OS   Pseudomonas sp. FGI182.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1259844 {ECO:0000313|EMBL:AHD12221.1, ECO:0000313|Proteomes:UP000018783};
RN   [1] {ECO:0000313|EMBL:AHD12221.1, ECO:0000313|Proteomes:UP000018783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI182 {ECO:0000313|EMBL:AHD12221.1,
RC   ECO:0000313|Proteomes:UP000018783};
RG   DOE Joint Genome Institute;
RA   Currie C., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP007012; AHD12221.1; -; Genomic_DNA.
DR   RefSeq; WP_025337202.1; NZ_CP007012.1.
DR   AlphaFoldDB; V9WML4; -.
DR   PATRIC; fig|1259844.3.peg.52; -.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   Proteomes; UP000018783; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          218..662
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   664 AA;  74534 MW;  FC75B32F30C6043D CRC64;
     MDNPLLQNSR IPVDYPSITL QNMQVAFDHV LLAHEQGIER IIRDQQALPT WDDMVLAVDG
     LDSQLLTVLY AASPLVGRDE AWAGAIFDFF AKATERFEQK FTNSALQALY ERLANSDIGK
     QLDAQKRATL RWHLHKFASS GASLDPAGKV RLAELLKQIG IAREAFRSNI NRPGLSITDE
     SELSGVPQRI RDELATRAQE AGEPGWLIAC ESVTTDAVLK HADNRQLRER VYRAYNTRGV
     GLGQQQDNRS HLEQLARLLE EKAHLLGFAS HLEQSLQMKS AGSVAQVRGF LHDLADHVRP
     AVLQWRADMQ RQAAAKGLGN VQPWDIAYLQ ASSREVLSTE ALRVHFPLNA VVSALQQLAE
     KLFGVTLLAK PLATWDDSVQ PFEVWQDNAL IGFLYLDAVQ HAGKQPDSVF TTYIRNRRVD
     AEGIFQAASV VVYSDVPAAL PGSQPLLDHL SLRKLFHEFG HALHHLLVRT TNHVMSNVTE
     LGTDGVELFG KLFERWVWDA DYLVEISSPL QDGSKLSRPR VDECLRRLRQ QGVEETARDL
     SMALFDLDLH GMPNDGRSLE QRLGDAREHC GYWPLAEFEH PAHAFDHLVN GYDAGYYAYL
     WSDVHAFDLF TRFEAQGLLD RATGRALQET LLAPGASRPL REGIEVFLGR QSSQLPFLRW
     HGLK
//