UniProt: E1SU21

Database: UniProt
Entry: E1SU21_FERBD

LinkDB:  E1SU21_FERBD 
Original site:  E1SU21_FERBD

All links

Ontology (4)   
   GO (4)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   SMART (1)   
All databases (16)   

Download RDF

ID   E1SU21_FERBD            Unreviewed;       449 AA.
AC   E1SU21;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   OrderedLocusNames=Fbal_0959 {ECO:0000313|EMBL:ADN75168.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75168.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN75168.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC   {ECO:0000313|Proteomes:UP000006683};
RX   DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA   Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA   Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002209; ADN75168.1; -; Genomic_DNA.
DR   RefSeq; WP_013344474.1; NC_014541.1.
DR   AlphaFoldDB; E1SU21; -.
DR   STRING; 550540.Fbal_0959; -.
DR   GeneID; 67181205; -.
DR   KEGG; fbl:Fbal_0959; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_0_2_6; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000006683; 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; 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; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
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:ADN75168.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006683};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        363..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        391..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        425..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          115..186
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   DOMAIN          210..279
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   449 AA;  48264 MW;  35A673B007010402 CRC64;
     MLAFVWNLGA FIVALGILVT VHEFGHFWVA RRCGVKVERF SIGFGKAIWR RTGADGTEYV
     VAMIPLGGYV KMLDGRVDDL APEMASQAFD RKPVWQRIAV VSAGPLANFA FALVALYAMY
     LVGVPAVRPV LDNPAPQSIA EQAGLEPKSL ITSVAGQEVL DWEAVNLALL GQLGQEHIAL
     TVETPGGGLR DVSLNTASWK VNPETQSILA SLGLVPWSPK ATDTLAFVDE SGAAYAAGVR
     QGDRLLALGD QPYQDWDELV AMVQAHADKP LAIEVERAGE RFSYTMVPKG ELENGQLVGK
     IGVAPGREDW PEAYRIDLKY GAFDALVKGA ERTWELTALT LKMIGNLFTG EVSVKSLSGP
     ISIAQGAGAT AGFGLVYFLG FLALISVNLG IINLLPLPVL DGGHLLYYFI ELLTGRPVPE
     RVQEIGFRIG SALLLLLMSI AIVNDVARL
//

DBGET integrated database retrieval system