ID A0A2I5TB57_SERS3 Unreviewed; 451 AA.
AC A0A2I5TB57;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=CWC46_19460 {ECO:0000313|EMBL:AUH01789.1}, Ser39006_019460
GN {ECO:0000313|EMBL:AUH06112.1};
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=104623 {ECO:0000313|EMBL:AUH06112.1, ECO:0000313|Proteomes:UP000017700};
RN [1] {ECO:0000313|EMBL:AUH06112.1, ECO:0000313|Proteomes:UP000017700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH06112.1}, and ATCC 39006 / SC
RC 11482 {ECO:0000313|Proteomes:UP000017700};
RX PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA Brugger K., Brown S.D., Salmond G.P.;
RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT for analysis of the biosynthesis and regulation of prodigiosin, a
RT carbapenem, and gas vesicles.";
RL Genome Announc. 1:E01039-E01039(2013).
RN [2] {ECO:0000313|EMBL:AUH06112.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH06112.1};
RA Wang G., Yang Y., Su Y.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AUH01789.1, ECO:0000313|Proteomes:UP000233778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH01789.1,
RC ECO:0000313|Proteomes:UP000233778};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUH06112.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH06112.1};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006.";
RL Submitted (NOV-2017) 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 ---------------------------------------------------------------------------
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; CP025085; AUH01789.1; -; Genomic_DNA.
DR EMBL; CP025084; AUH06112.1; -; Genomic_DNA.
DR RefSeq; WP_021014879.1; NZ_CP025085.1.
DR AlphaFoldDB; A0A2I5TB57; -.
DR STRING; 104623.Ser39006_01611; -.
DR KEGG; sera:Ser39006_019460; -.
DR KEGG; serq:CWC46_19460; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000017700; Chromosome.
DR Proteomes; UP000233778; 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; -; 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.
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:AUH06112.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017700};
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 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 201..291
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 451 AA; 49444 MW; A998D21261251A75 CRC64;
MMNILWNLAA FIIALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RYDRHGTEYV
IALIPLGGYV KMLDGRIDNV PTALFHQAFN NKTVLQRAAI VSAGPIANFI FAVFAYWMVF
IIGVPGIRPV VGEVLPDSIA SHAQISPGME LKTIGGIETP DWDSARLALI GKIGDPEVII
GTAPLGSSQI ERKTLNLRDW HFEPDKQDPA VSLGIVPRGP QIDAVLTQVQ PHSAAEKAGL
DVGDRIVKVD GQPLTRWQQF VTTIRDNPGN VVTLEVERGG ETLTLSLTPD KKSVGQGQYV
GFAGVVPRVI PLPDEYRTVR QYGPFGAIYE ASDKTWQLMK LTVSMLGKLI TGDITLNNLS
GPISIAQGAG MSADYGLIYY LMFLALISVN LGVINLFPLP VLDGGHLLFL VLEKLKGKPV
SERVQNFGYR IGTVLLMMLM GLALFNDFSR L
//
