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Database: UniProt
Entry: A0A1Z3HTQ1_9CYAN
LinkDB: A0A1Z3HTQ1_9CYAN
Original site: A0A1Z3HTQ1_9CYAN 
ID   A0A1Z3HTQ1_9CYAN        Unreviewed;       375 AA.
AC   A0A1Z3HTQ1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=XM38_046130 {ECO:0000313|EMBL:ASC73642.1};
OS   Halomicronema hongdechloris C2206.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC   Halomicronema.
OX   NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC73642.1, ECO:0000313|Proteomes:UP000191901};
RN   [1] {ECO:0000313|EMBL:ASC73642.1, ECO:0000313|Proteomes:UP000191901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2206 {ECO:0000313|EMBL:ASC73642.1,
RC   ECO:0000313|Proteomes:UP000191901};
RX   PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA   Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA   Scheer H., Willows R.D., Chen M.;
RT   "Characterization of red-shifted phycobilisomes isolated from the
RT   chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL   Biochim. Biophys. Acta 1857:107-114(2016).
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; CP021983; ASC73642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z3HTQ1; -.
DR   KEGG; hhg:XM38_046130; -.
DR   OrthoDB; 166377at2; -.
DR   Proteomes; UP000191901; 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; 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; 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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000191901};
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        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        77..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        106..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        132..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        191..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          314..373
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   375 AA;  39907 MW;  23B1D016F2354EFC CRC64;
     MNGNIRVGSL LGIPFYINVS WFLVLALVTW SYGSGLAFEF PNLPGITPWI MGLVAALLLF
     ASVLAHELGH SIAARRQGVG VRSITLFLFG GLAALEKESD TPSGAFWVAI AGPLVSLALF
     FGLSLTNSVL PLAGPLSAVL GLLAYINLIL AAFNLIPGLP LDGGNVLKAL VWKLTGNAYK
     GVEIASRVGQ FFGWTAIVLG VLSVLGISQV GSIWTLLIGF FLLQNANRSA QYAEVQARLD
     GLTAADVVTP DSPVVAQSAT LREFADEAVL SAGSQWRKFL VIDDEGQLVG TLAVDILRQI
     PREDWAQVRV CDRMDPLEGI ETVDSDRPLL DVLGKLEESQ IPALVVTKAN GMLVGLLERS
     AVIRLLQQGS TPNPA
//
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