ID   HTPX_PELPB              Reviewed;         291 AA.
AC   B4SCH3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Ppha_1962;
OS   Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=324925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5477 / BU-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001110; ACF44178.1; -; Genomic_DNA.
DR   RefSeq; WP_012508659.1; NC_011060.1.
DR   AlphaFoldDB; B4SCH3; -.
DR   SMR; B4SCH3; -.
DR   MEROPS; M48.002; -.
DR   EnsemblBacteria; ACF44178; ACF44178; Ppha_1962.
DR   KEGG; pph:Ppha_1962; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_1_0_10; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   Proteomes; UP000002724; 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..291
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000098830"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        38..58
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        199..219
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         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   291 AA;  31308 MW;  011BC82B0C1E4248 CRC64;
     MKRVILFLLT NFAVMLVLSV TARILGVDRF LTSNGLNMGM LLVFAALIGF GGSFISLLMS
     KTMAKWSTGA QVIKQPSSQE EVWLVETVRR LSTKAGFAMP EVAIYDGAPN AFATGPSKSR
     SLVAVSTGLL HSMDRKQVEA VLAHEVSHIN NGDMVTLTLI QGVLNTFVIF LSRIIAYAVD
     SFLRRDEDES GSPGIGYWIS SIACEILFGI LASIVVMFFS RKREYRADAG AAALMGDRRP
     MIDALRALGN LDAGQLPKEM AASGIAGGGM MALFSSHPPL ESRIAALESA R