ID Q1MRD3_LAWIP Unreviewed; 374 AA.
AC Q1MRD3;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN OrderedLocusNames=LI0387 {ECO:0000313|EMBL:CAJ54443.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54443.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54443.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54443.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54443.1; -; Genomic_DNA.
DR RefSeq; WP_011526472.1; NC_008011.1.
DR AlphaFoldDB; Q1MRD3; -.
DR STRING; 363253.LI0387; -.
DR KEGG; lip:LI0387; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_7; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000002430; Chromosome.
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; -; 1.
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; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
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:CAJ54443.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 298..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 135..203
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 374 AA; 41274 MW; DE157FED54A710A7 CRC64;
MDFLQTFVSQ WNNALAVVVV LGALIFFHEL GHFMMARILG IGVKTFSLGF GPKIFTIGKR
KTKYSLSLIP LGGYVSLAGE EDEDENKKIE QSSQITDELF LPTEKFSNRP PWHRLLVVLA
GPVANILLAF FIYWGVSWVQ GSTFLLPIIG TITENSPAEH AGLLPGDIIT RVDGMPVSQW
DQVAEYIAES QGNEVTITLS RDDKLLEFRL TPEEKSRTNL FGEKKPAWLI GISAQGDIET
RPLSFLAASV TGLKKTWFSI SFTCESLLKL FQKVVPLDSI GGPILIAQLV GQQANAGIIP
LLLLTALISI NLGVLNLLPI PILDGGHVVF LLLEMIFQRP ISPFIKTVSM RIGIVLLLSL
MVFATWNDIM RLVS
//
