ID A0A1E3GRX0_9GAMM Unreviewed; 445 AA.
AC A0A1E3GRX0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rseP {ECO:0000313|EMBL:ODN66326.1};
GN ORFNames=A9E74_01974 {ECO:0000313|EMBL:ODN66326.1};
OS Methylophaga muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN66326.1, ECO:0000313|Proteomes:UP000094379};
RN [1] {ECO:0000313|EMBL:ODN66326.1, ECO:0000313|Proteomes:UP000094379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bur 1 {ECO:0000313|EMBL:ODN66326.1,
RC ECO:0000313|Proteomes:UP000094379};
RA Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA Mustakhimov I., Trotsenko Y.A.;
RT "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN66326.1}.
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DR EMBL; MCRI01000022; ODN66326.1; -; Genomic_DNA.
DR RefSeq; WP_069296397.1; NZ_MCRI01000022.1.
DR AlphaFoldDB; A0A1E3GRX0; -.
DR STRING; 291169.A9E74_01974; -.
DR PATRIC; fig|291169.3.peg.1984; -.
DR Proteomes; UP000094379; Unassembled WGS sequence.
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; PF00595; PDZ; 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:ODN66326.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094379};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 369..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 192..250
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 445 AA; 48119 MW; 02F84C50BC4E1BFB CRC64;
MQSLIFFIIA LSLLVVIHEF GHYWVARRCG VKVLRFSVGF GQKLWSKQLK NGTEFVIAAL
PLGGYVKMLD EREAPVAENE LEQTFNRQPL RNRVAIVSAG PIANLLFAVF AYWMIMVIGV
PGMKPIIAEV TANSPAAAAQ LYAGEEIIAV NGKATPTVNS LFQQWLRLAQ SGETITLTTR
SADVETNKQL TLPKLGLDDA GSLFNQIGIT TVQPEMPPVL DNIVADSPAE KAGLQAGDEL
ISADGKTLSS WQAWVSLIQS NADTAMNIEI LRNGEIQQLV ITPAADENGV GRIGAAVNTD
AYEIPAELRS ELRYGPLAAI PQAFTQTWQF SVTTLSGLWG MLVGTVSSDN LGGPIAIAQF
AGDSAQQGLI AFISFLAMIS ISLGILNLLP VPVLDGGHLL MYFFEWIRGK PLPESVQIQG
QKIGLFLILL LMVFAFTNDI VRLIG
//