ID   HTPX_KINRD              Reviewed;         294 AA.
AC   A6W5R0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Krad_0660;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
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DR   EMBL; CP000750; ABS02149.1; -; Genomic_DNA.
DR   RefSeq; WP_012085009.1; NC_009664.2.
DR   AlphaFoldDB; A6W5R0; -.
DR   STRING; 266940.Krad_0660; -.
DR   EnsemblBacteria; ABS02149; ABS02149; Krad_0660.
DR   KEGG; kra:Krad_0660; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_3_1_11; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   Proteomes; UP000001116; 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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..294
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000077465"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   294 AA;  31640 MW;  67632AE25C39F981 CRC64;
     MHRHHNGLKT AVLFGGIWGV LLLIGAFLAS SFRSPGVLLV FVVIGLATSA YSYWNSAGLA
     LRAMRARPVS EAEQPGMHRI VRELSTAARQ PMPQLYVSPT MAPNAFATGR NPENAAVCCT
     EGILQLLDER ELRGVLGHEL MHVYNRDILT SSVAGALAGV ITSIAQFGVF FGSALGGGRD
     GEERANPLAL LLLSLMAPLA ASVIQLAISR TREYDADEDG ARLTGDPLAL ASALRKLELG
     TRQLPLPPER ELVNSSHMMI ANPFRGQGVA RLFSTHPPMA ERIARLEALA GYRR