ID HTPX_NOSP7 Reviewed; 289 AA.
AC B2J204;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Npun_R3611;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RX PubMed=23463784; DOI=10.1104/pp.112.213116;
RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT Cyanobacterium-Plant Symbiosis.";
RL Plant Physiol. 161:1984-1992(2013).
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; CP001037; ACC82006.1; -; Genomic_DNA.
DR RefSeq; WP_012409978.1; NC_010628.1.
DR AlphaFoldDB; B2J204; -.
DR SMR; B2J204; -.
DR EnsemblBacteria; ACC82006; ACC82006; Npun_R3611.
DR KEGG; npu:Npun_R3611; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_3_0_3; -.
DR OrthoDB; 15218at2; -.
DR PhylomeDB; B2J204; -.
DR Proteomes; UP000001191; 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 CDD; cd07336; 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; IPR022919; Pept_M48_protease_HtpX.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 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..289
FT /note="Protease HtpX homolog"
FT /id="PRO_1000098829"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 31..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 289 AA; 30546 MW; E147F75B4E311B42 CRC64;
MGNQVKTAAL LAALSGLLIA ISYWVIGGSS GLIIGIGLAA VTNLFSWYQS DKIALAVYQA
QPVSEGEAPG LYRMVQRLSD RANIPMPRVY IVPSQGANAF ATGRDPEHAA VAVTEGILNI
LPDDELEGVI AHELTHIINR DTLTQAVAAT VAGAISFLAQ MVSYSLWFGG GSRDDNRGAN
PLGVLLTVML APLAATIIQL AISRTREFSA DAGSARLTGN PRALARALQR LEALAKQIPL
NANPAFEPLL IINSISGQFL GNLFSSHPAT EARVAALLKL EQQLPTKAY
//
