ID A0A0Q4YB99_9BURK Unreviewed; 453 AA.
AC A0A0Q4YB99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=ASF43_07580 {ECO:0000313|EMBL:KQP17734.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP17734.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP17734.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP17734.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP17734.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP17734.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP17734.1}.
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DR EMBL; LMMV01000012; KQP17734.1; -; Genomic_DNA.
DR RefSeq; WP_056181376.1; NZ_LMMV01000012.1.
DR AlphaFoldDB; A0A0Q4YB99; -.
DR STRING; 1736316.ASF43_07580; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000051560; 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; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 2.
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 SUPFAM; SSF50156; PDZ domain-like; 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:KQP17734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051560};
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 380..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 433..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 6..438
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 226..269
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 453 AA; 48684 MW; 45AB1353FBA0164C CRC64;
MLTIVAFVVA LGLLIAVHEY GHYRVAVACG VKVQRFSIGF GKVLLRWQPK GSPTEFVIGA
FPLGGYVKML DEREGPVAPE ERHRAFNTQT VGKRAAIVGA GPAANLLLAV LLYAVVNWSG
IDEPRAVLAS PITASIAERA GVRGGEVVTQ AAWDGDELRP VRSFEELRWL LTRGALDGHD
VRLEVASGAQ GQRRELLLPL GQIGARDADA GLFRRIGIVA PWTQPVIGDV MPDGAGAAAG
LRSGDVVRAI GATSIVDGQQ LREAIRASVR GEQGMAQRWR VERDGRALEL DVTPQPQREG
EAWIGRIGAY VGAPPAMVTV HHGPLEGLWN GVVRTWEVSS LTLRMMGRMV IGEASLKNLS
GPLTIADYAG KSASLGLTQY LVFLALISVS LGVLNLLPLP VLDGGHLMYY LWEAVTGKSV
SDAWMERMQR TGVALLLVMM SIALFNDVTR IFG
//
