ID A0A0U5H539_9EURY Unreviewed; 390 AA.
AC A0A0U5H539;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN ORFNames=HHUB_3456 {ECO:0000313|EMBL:CQH61460.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH61460.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(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|ARBA:ARBA00004651,
CC ECO:0000256|PIRNR:PIRNR006404}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR006404}.
CC Membrane {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; LN831302; CQH61460.1; -; Genomic_DNA.
DR RefSeq; WP_059057796.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5H539; -.
DR STRING; 1407499.HHUB_3456; -.
DR GeneID; 26660067; -.
DR KEGG; hhb:Hhub_3456; -.
DR OrthoDB; 12044at2157; -.
DR Proteomes; UP000066737; Chromosome I.
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; cd04801; 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; STAGE IV SPORULATION PROTEIN FB; 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 Reference proteome {ECO:0000313|Proteomes:UP000066737};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 153..171
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 205..233
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 255..310
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 317..375
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 390 AA; 41927 MW; 313A77E52D027834 CRC64;
MRSFKIGSAF GIPIKLDVTF LLILPVFAYL IGMQVDIWVE TLNGVPFNAN LNPAALTDGN
MRWYLGVAGA VGLFAGVVLH ELGHSVVAMR FGFPIDSITL WILGGIASLS DQPEEWSQEF
WIAVAGPVVS IALGVLSLGA LHFLPASLDT VRFVFGYLAL MNFALAAFNL LPGFPMDGGR
VLRALLARKR SFARATQIAA EVGKLFALVL GIVGLLGFNL ILIAIAFFIY VGASGEAQRT
VMNAAFQDVS VADIMTHDVH TVEADDSVAE LMERMLEQRH TGYPVMRQGS VAGMVTLDDA
RDVNAVERDA IRVEDVMSED VYTIPRASNA MDALDAMQEQ GVGRLVVVDE DGEMVGLVSR
TDLMTAFDII QSTGVGEEPK LSTASGQSTP
//