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Database: UniProt
Entry: A7I4U7_METB6
LinkDB: A7I4U7_METB6
Original site: A7I4U7_METB6 
ID   A7I4U7_METB6            Unreviewed;       296 AA.
AC   A7I4U7;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
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   OrderedLocusNames=Mboo_0236 {ECO:0000313|EMBL:ABS54758.1};
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS54758.1, ECO:0000313|Proteomes:UP000002408};
RN   [1] {ECO:0000313|Proteomes:UP000002408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8
RC   {ECO:0000313|Proteomes:UP000002408};
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS54758.1; -; Genomic_DNA.
DR   RefSeq; WP_011991246.1; NC_009712.1.
DR   AlphaFoldDB; A7I4U7; -.
DR   STRING; 456442.Mboo_0236; -.
DR   GeneID; 5411062; -.
DR   KEGG; mbn:Mboo_0236; -.
DR   eggNOG; arCOG01331; Archaea.
DR   HOGENOM; CLU_042266_0_2_2; -.
DR   OMA; REYMADS; -.
DR   OrthoDB; 28389at2157; -.
DR   Proteomes; UP000002408; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
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; PF01435; Peptidase_M48; 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   Reference proteome {ECO:0000313|Proteomes:UP000002408};
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..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        150..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          77..289
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   296 AA;  32787 MW;  989E3C88F7CDCB82 CRC64;
     MEWKRDWGLT ARVLLTGFLL FILYLVFMTV LVIFFPGVSI WLIVGLAVVM GGIQYFFSDK
     LVLWSTHARI ISEDEYPDLH QTVAKLVHEA DLPMPKIAIM QSPVPNAFAT GRSPKHAVVC
     CTDSIMRLLS RDELEAVLAH ELSHVKNRDI LTMALASFVA MIASMIMQSV FFSALFGGNS
     RDNGAGWIIV WVVSILVYAL STLLMLALSR YREFAADRGS ALITRNPRAL ISALNKISGR
     MEVVPPDAKA KVEGANAFFI IPALSGNTLM ELFSTHPPIE KRIAALEKIA AELRIN
//
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