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Database: UniProt
Entry: A0A0U3CHA8_9EURY
LinkDB: A0A0U3CHA8_9EURY
Original site: A0A0U3CHA8_9EURY 
ID   A0A0U3CHA8_9EURY        Unreviewed;       319 AA.
AC   A0A0U3CHA8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Protease HtpX homolog {ECO:0000256|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   ORFNames=sm9_0123 {ECO:0000313|EMBL:ALT67932.1};
OS   Methanobrevibacter millerae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=230361 {ECO:0000313|EMBL:ALT67932.1, ECO:0000313|Proteomes:UP000067738};
RN   [1] {ECO:0000313|EMBL:ALT67932.1, ECO:0000313|Proteomes:UP000067738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM9 {ECO:0000313|EMBL:ALT67932.1,
RC   ECO:0000313|Proteomes:UP000067738};
RA   Leahy S.C., Kelly W.J., Pacheco D.M., Li D., Altermann E., Attwood G.T.;
RT   "The complete genome sequence of the rumen methanogen Methanobrevibacter
RT   millerae SM9.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|ARBA:ARBA00009779, ECO:0000256|HAMAP-Rule:MF_00188}.
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DR   EMBL; CP011266; ALT67932.1; -; Genomic_DNA.
DR   RefSeq; WP_058738296.1; NZ_CP011266.1.
DR   AlphaFoldDB; A0A0U3CHA8; -.
DR   GeneID; 26735103; -.
DR   KEGG; mmil:sm9_0123; -.
DR   PATRIC; fig|230361.4.peg.124; -.
DR   OrthoDB; 28389at2157; -.
DR   Proteomes; UP000067738; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07338; M48B_HtpX_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00188}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        148..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        177..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          265..291
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   319 AA;  35753 MW;  2952361469CB14D6 CRC64;
     MKGTWKLKLR MILTSVFMFS IVYFLVLLVA RYMGISSWRL YMGVSLVIVF AQYWFGPTLV
     KHSMNVRPLS EAEAPHIHKM VAELAQEAGV PKPEVGLSEI NIPNAFAYGR TSRSGHIAIT
     RPILGLLDYD ELRAVLGHEM GHIKHNDMAV TAAVSVIPMV CYYIAIAFMF SRDNENGAGI
     IIGLLGYVFY LIGQLLVLFI SRTREYYADE ASVEFGNRPA ALVSALYKLS YGASRCSQET
     IKELNTNRAF FATDINNAQH DIDDFSQVDF DGDGKISDEE LKRLANSDIK ISKTKGIMEL
     LSTHPDSLKR VKRLAELEN
//
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