ID D5H7Z2_SALRM Unreviewed; 391 AA.
AC D5H7Z2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN Name=SpoIVFB {ECO:0000313|EMBL:CBH24147.1};
GN OrderedLocusNames=SRM_01226 {ECO:0000313|EMBL:CBH24147.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH24147.1, ECO:0000313|Proteomes:UP000000933};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M8;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-95(2010).
RN [2] {ECO:0000313|EMBL:CBH24147.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH24147.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [3] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR006404}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|PIRNR:PIRNR006404}.
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DR EMBL; FP565814; CBH24147.1; -; Genomic_DNA.
DR RefSeq; WP_013061605.1; NC_014032.1.
DR AlphaFoldDB; D5H7Z2; -.
DR KEGG; srm:SRM_01226; -.
DR PATRIC; fig|761659.10.peg.1353; -.
DR HOGENOM; CLU_037123_1_1_10; -.
DR Proteomes; UP000000933; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02163; Peptidase_M50; 2.
DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006404};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR006404};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006404}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 99..122
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 192..218
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 240..296
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 302..359
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 391 AA; 41660 MW; CEEA16D16B87E280 CRC64;
MKRSLRVGSV TGIGIFLHWT FLLLVAAIFA YYYVQSQSLG AALSGMGLIL GVFVCVILHE
LGHALTARRF GVPTRSITLY PIGGLARLER IPSEPMKEFW IAIGGPAVNV VIAFALALVL
LVTGGTLAPV ALEAPGSHAL ASLMWINAVL AVFNMLPAFP MDGGRVLRAL LALRWDYAQA
TQTAANVGQG MAVLFGLVGI MTWNPVLLFI ALFVYVGAQQ ESKQAMYRAF TEGTPVREAM
VTRFATLTVD DTLDDAVDAL LAGTDHDFPV LEAGTVVGLL RRKQLIQALS EHGRDTPVAE
VADADCFTTA PSAPLDEVFQ QMNARSCSTV PVVDGGQLVG LLTLENVGEL IMVSSALETR
SHSRVPRDQL SEAPLRERPD GAASSGAPPV P
//
