ID E3EHF2_PAEPS Unreviewed; 423 AA.
AC E3EHF2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=yluC {ECO:0000313|EMBL:ADO56105.1};
GN ORFNames=PPSC2_10065 {ECO:0000313|EMBL:ADO56105.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56105.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO56105.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO56105.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO56105.1; -; Genomic_DNA.
DR RefSeq; WP_013370715.1; NC_014622.2.
DR AlphaFoldDB; E3EHF2; -.
DR STRING; 1406.LK13_22535; -.
DR KEGG; ppm:PPSC2_10065; -.
DR PATRIC; fig|886882.15.peg.2121; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000006868; 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; 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; PF13180; PDZ_2; 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}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 194..241
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 423 AA; 47042 MW; B075330B17A17F64 CRC64;
METIQIVLMT VLMFFVIVTV HEWGHYYFAK RAGILVREFA IGFGPKLFSY KRNETRFTLR
LLPFGGFARM AGEDPEVNEI ETGQTIAVRV TDGVVKTIYL DQLDNRKNVV RGEVLDIDLE
QALTVKLDVD GEDQQYTVHP QAMMVTKGQS IQIAPKDRQY GSKTVGQRAM AIFAGPLMNF
ILAFILFGLH IQMVGIQVDN PTYVQISEIT AGMPAAEADL HKGDIIESVN GVAIGANVEN
MIKLIADSQD KPMKWTVRRD DKTFDLTITP RAMEGQKGGK VGIVPELPKR QAGVGETFKF
AGQSMVRTTD IIFQGFSQLI QRFSINDLGG PVRTFEVTGQ IAKQGIEQLT YWTAIMSLYL
GIFNLLPIPA LDGSRLVFLG VEAVRGRPVD PSREGMVHFV GFAMLFLLMI AVTYNDILRL
ING
//
