ID I0GLT7_SELRL Unreviewed; 282 AA. AC I0GLT7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-NOV-2024, entry version 60. 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; Bacillota; 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}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. CC -!- SIMILARITY: Belongs to the peptidase M48B family. CC {ECO:0000256|ARBA:ARBA00009779, ECO:0000256|HAMAP-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; AP012292; BAL81724.1; -; Genomic_DNA. DR RefSeq; WP_014423171.1; NC_017068.1. DR AlphaFoldDB; I0GLT7; -. DR KEGG; sri:SELR_00160; -. DR PATRIC; fig|927704.6.peg.17; -. DR eggNOG; COG0501; Bacteria. DR HOGENOM; CLU_042266_3_0_9; -. DR OrthoDB; 15218at2; -. DR Proteomes; UP000007887; 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; IPR050083; HtpX_protease. 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. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00188}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00188}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00188}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00188}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00188}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_00188}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00188}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00188}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00188}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00188}. 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 BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="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 //