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Database: UniProt
Entry: E4RT34_LEAB4
LinkDB: E4RT34_LEAB4
Original site: E4RT34_LEAB4 
ID   E4RT34_LEAB4            Unreviewed;       442 AA.
AC   E4RT34;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   OrderedLocusNames=Lbys_2046 {ECO:0000313|EMBL:ADQ17742.1};
OS   Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS   106382 / 4M15).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ17742.1, ECO:0000313|Proteomes:UP000007435};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Leadbetterella byssophila DSM 17132.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ17742.1, ECO:0000313|Proteomes:UP000007435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC   {ECO:0000313|Proteomes:UP000007435};
RX   PubMed=21475582; DOI=10.4056/sigs.1413518;
RA   Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Leadbetterella byssophila type strain
RT   (4M15).";
RL   Stand. Genomic Sci. 4:2-12(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; CP002305; ADQ17742.1; -; Genomic_DNA.
DR   RefSeq; WP_013408788.1; NC_014655.1.
DR   AlphaFoldDB; E4RT34; -.
DR   STRING; 649349.Lbys_2046; -.
DR   KEGG; lby:Lbys_2046; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_0_0_10; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000007435; 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:InterPro.
DR   CDD; cd00989; PDZ_metalloprotease; 2.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 2.
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; 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}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007435};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        39..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        370..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        418..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          229..258
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   442 AA;  49553 MW;  0455624DC209E7FE CRC64;
     MNGLIMAAQL LLALTILVGL HEFGHFLFAR IFKIRVNKFY IFFDFLFPLP NVLNFSLWKK
     KVGDTEYGLG WFPLGGYVDI AGMVDETKDA SQLSAEPQPW EFRSKPAWQR LFVMLGGIIV
     NVILGMMIYT GVKYVWGDTD YAKEELNKSG IFAYPVAEKI GLQTGDKIIK INGSDYKYFS
     DITAAIVKEN TTFTIEREGK TFDVYVPNEL IDDVAKKKMF ITPLFEFDIL NVMKGSPAEE
     SGLRAGDKVI SLNGEPVKYY QLFTPKLRTY AGKKVELGIL RDGTELTIQP TVSADSTIGF
     TMNPLLKVTK SEFTFGEAVV EGSKEALSII PQQINGFSRI FKGHISPQNA LTGPVGLAQM
     FSPQWDWEKF WILTGMLSMA LAFMNALPIP ALDGGHVVML IYEMIAGKAP SEKFMERTQQ
     VGTFILLALM LYVLFNDTVK LF
//
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