ID A0A0S8BEF3_9PROT Unreviewed; 372 AA.
AC A0A0S8BEF3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN ORFNames=AMJ68_10665 {ECO:0000313|EMBL:KPK09929.1};
OS Acidithiobacillales bacterium SG8_45.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK09929.1, ECO:0000313|Proteomes:UP000053136};
RN [1] {ECO:0000313|EMBL:KPK09929.1, ECO:0000313|Proteomes:UP000053136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK09929.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK09929.1}.
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DR EMBL; LJTU01000073; KPK09929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BEF3; -.
DR PATRIC; fig|1703383.3.peg.174; -.
DR Proteomes; UP000053136; Unassembled WGS sequence.
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; 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 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..35
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 107..132
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 183..207
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 250..306
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 313..372
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 68
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 372 AA; 40697 MW; 35F35D8ADA91A99E CRC64;
MFENAIRLGT VAGIRIGVHY TWFAIFLLLT TTLYGSFTHQ HPDWDKFTAL LTAIVTALIF
FASIVLHELG HSIVAIRRGI SVRSITLFIF GGVAQTEKEA ESAQTEFMVA IAGPLVSIAL
AGLFYLLSVW LAPINEIAAE AFDWLATINF MVAIFNMAPG FPLDGGRVFR ALVWGISGDA
SKGMRWAVFS GKAVAYLLIG LGAMIALQAN LISGIWFIGI GWFLLISAQA SGQSFTINRV
FSQSVARDVM VRDVPVVDSG TSIADWVEDY VFSKGTRAFL VAEQDDIIGL ITLSDCSRIP
REQWAETAVK MVMTPVGQLR TVKVDTDINT VLQLLAAQSL NQVPVVEDSA IVGWIDRERL
IKILRLHTEA GE
//
