ID A0A0C2QKJ5_9CYAN Unreviewed; 374 AA.
AC A0A0C2QKJ5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN ORFNames=SD81_06045 {ECO:0000313|EMBL:KIJ78850.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ78850.1};
RN [1] {ECO:0000313|EMBL:KIJ78850.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ78850.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIJ78850.1}.
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DR EMBL; JXCB01000004; KIJ78850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2QKJ5; -.
DR OrthoDB; 166377at2; -.
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; cd04639; CBS_pair_peptidase_M50; 1.
DR CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; 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 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 107..128
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 191..214
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 248..309
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 313..374
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 67
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 70
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 374 AA; 40026 MW; 6AEA07741E400A02 CRC64;
MNGTIRVGNL FGIPFYIHPS WFLVLGLVTW SYSSGLAAQF PQLAGGLALL LGLLTALLLF
SSVVAHELGH SFVAIRQGID VKSITLFIFG GLASLERESK TPGEAFWVAI AGPSVSLLLF
SLFTALGFAT AASGALAAIL GVLASVNLAL ALFNLIPGLP LDGGNILKAF VWKVTGNPYK
GVVFASRVGQ IFGWVAIASG LVPLLLFGSF GNFWNALVGF FLLQNAGNAA QFARVQERLT
GLTAADAVTS DSPIVSATLT LREFADERIL NWQNWHRFLV TDDNGQLVGA ISINDLRTIP
TTLWSETQIK EIMRPVEDFT TVKSDQPLLE VVKLLEQGKL SALAVIRDNG VLVGILEKAS
IINLLEKRAQ PNPA
//
