ID A0A448TRW2_9PAST Unreviewed; 443 AA.
AC A0A448TRW2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rseP {ECO:0000313|EMBL:VEJ08774.1};
GN ORFNames=NCTC12871_00189 {ECO:0000313|EMBL:VEJ08774.1};
OS Actinobacillus delphinicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=51161 {ECO:0000313|EMBL:VEJ08774.1, ECO:0000313|Proteomes:UP000279799};
RN [1] {ECO:0000313|EMBL:VEJ08774.1, ECO:0000313|Proteomes:UP000279799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12871 {ECO:0000313|EMBL:VEJ08774.1,
RC ECO:0000313|Proteomes:UP000279799};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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DR EMBL; LR134510; VEJ08774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448TRW2; -.
DR KEGG; adp:NCTC12871_00189; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000279799; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 2.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:VEJ08774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000279799};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 419..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 206..254
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 443 AA; 48938 MW; 7757C6BC1C8AE4EB CRC64;
MTVVWSVLGF VVAISILVAF HEYGHFWAAR RCGVKIERFS IGFGKILWRR VGKSGTEFAI
SAIPLGGYVK MLDERQEDVP EALKPYAFNN KTVWQRMFIV SAGPIANLLL AVVLYAVVLM
IGIPTLKPVI AGVVPHSIAQ QANLPLDTQI TAIDGEPVED WDTINMLLAS KIGEKQVDLT
LTSLTDRRSI HKKLDIRGWQ YDEEKKSAFG ALGIEPVMPT VYMKLSRVVK NSPAERAGLQ
VGDQLMQPNG RNIQWDTFIQ EVEKGNPIPV SVVRKDDVFN TTITPVKNEQ GRFMVGLAPS
VKPIDAIYRT VLRANPWQAL KQGVEKTANL SWLTIKVIGK LLTGQLSAKN LSGPISIAKG
AGMMAQIGLV YYLSFLAVIS VNLGIMNLFP LPVLDGGHLL FLIIESIKRK PVSERVQQVA
YQIGAILLLM LTAFALFNDL LRL
//
