HTPX_JANMA
ID HTPX_JANMA Reviewed; 290 AA.
AC A6SXH1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
GN Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=mma_1278;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00188};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00188};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
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DR EMBL; CP000269; ABR89198.1; -; Genomic_DNA.
DR RefSeq; WP_012079135.1; NC_009659.1.
DR AlphaFoldDB; A6SXH1; -.
DR SMR; A6SXH1; -.
DR STRING; 375286.mma_1278; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; ABR89198; ABR89198; mma_1278.
DR KEGG; mms:mma_1278; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_4; -.
DR OMA; AVCCTEG; -.
DR OrthoDB; 1918093at2; -.
DR BioCyc; JSP375286:MMA_RS06650-MON; -.
DR Proteomes; UP000006388; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR InterPro; IPR022919; Pept_M48_protease_HtpX.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..290
FT /note="Protease HtpX homolog"
FT /id="PRO_1000020875"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 290 AA; 30859 MW; AB63F6AB1609F9E7 CRC64;
MKRIFLFIAT NIAVIAVMSV VLSLLGVDRF ISQAGLNLPM LLVFSLVVGF TGSIISLLIS
KPMAKWSTGA RVIDAPSSST ELWLIDTVSK LAQRAGIKMP EVAVYDGEPN AFATGAFRDS
ALVAVSTGLL QSMTKDEVEA VLAHEVAHVA NGDMVTMTLV QGVVNTFVVF LSRVVGYFVD
RAISRDNNNS QGIGYTITVI VSQIVFGIAA SVIVAWFSRH REFRADAGAA KLLGSPQPMM
KALARLGGIE PTSLPEGLAS LGINDKPGFA ALFSSHPPIE DRIAALRSLQ