ID   I0GLT7_SELRL            Unreviewed;       282 AA.
AC   I0GLT7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   11-DEC-2019, entry version 42.
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=SELR_00160 {ECO:0000313|EMBL:BAL81724.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL81724.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL81724.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00188}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000256|HAMAP-
CC       Rule:MF_00188, ECO:0000256|SAAS:SAAS00541274}.
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DR   EMBL; AP012292; BAL81724.1; -; Genomic_DNA.
DR   RefSeq; WP_014423171.1; NC_017068.1.
DR   STRING; 927704.SELR_00160; -.
DR   MEROPS; M48.004; -.
DR   EnsemblBacteria; BAL81724; BAL81724; SELR_00160.
DR   GeneID; 31521286; -.
DR   KEGG; sri:SELR_00160; -.
DR   PATRIC; fig|927704.6.peg.17; -.
DR   KO; K03799; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   BioCyc; SRUM927704:G1H8D-17-MONOMER; -.
DR   Proteomes; UP000007887; 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   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 {ECO:0000256|HAMAP-Rule:MF_00188};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00423899};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00112036};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00016464};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00473692};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00112271};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00473645,
KW   ECO:0000313|EMBL:BAL81724.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016455};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016434};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00473636}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        140..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          66..277
FT                   /note="Peptidase_M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   METAL           130
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   METAL           134
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   METAL           201
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   282 AA;  30629 MW;  206AC2B99C5A60C4 CRC64;
     MNNLKTLMLM VLLGAMMIFI GGMVGGKSGM MIMLMISLGM NMFSYWFSDS MVLKMYNARE
     VSRADAPQLY GLVENLAANA QLPMPRVYII NEDTPNAFAT GRNPSHAAVA VTTGIMQALD
     YNELSGVLGH ELAHVKNRDI LTGTIAAMMA TVISYAAQFV AFFGGRSDDD EGGNPIAALL
     MVILAPIAAS LIQMAISRSR EYEADHDGAV ICGNANYLAD ALEKIEYYAL HGRQMSDATP
     ATAHMFIINP FSGAMSSMKK LFSTHPETRE RIARLRAQAN GR
//