ID A0A0G3EE81_9BACT Unreviewed; 376 AA.
AC A0A0G3EE81;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Putative protease HtpX {ECO:0000313|EMBL:AKJ64766.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:AKJ64766.1};
GN Name=htpX_2 {ECO:0000313|EMBL:AKJ64766.1};
GN ORFNames=L21SP4_01521 {ECO:0000313|EMBL:AKJ64766.1};
OS Kiritimatiella glycovorans.
OC Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC Kiritimatiellaceae; Kiritimatiella.
OX NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ64766.1, ECO:0000313|Proteomes:UP000035268};
RN [1] {ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of the first cultured
RT representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKJ64766.1, ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ64766.1,
RC ECO:0000313|Proteomes:UP000035268};
RX PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA Klenk H.P.;
RT "Characterization of the first cultured representative of Verrucomicrobia
RT subdivision 5 indicates the proposal of a novel phylum.";
RL ISME J. 10:2801-2816(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CP010904; AKJ64766.1; -; Genomic_DNA.
DR RefSeq; WP_052882062.1; NZ_CP010904.1.
DR AlphaFoldDB; A0A0G3EE81; -.
DR STRING; 1307763.L21SP4_01521; -.
DR KEGG; vbl:L21SP4_01521; -.
DR OrthoDB; 9781930at2; -.
DR Proteomes; UP000035268; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000035268};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 23..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..165
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 169..370
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 376 AA; 41924 MW; FEA77AC2CC2D0CE9 CRC64;
MTQEHPQPAD PEKARQYERM QHTLFAVKII AGAALLAAYQ LSGMSETLAA GLRLRFGAWP
VVNGAYILIS VFGMAAILFP LSYYGDFVLE HQFGMSRQRF SSWMTDYLKS LAIDLVFALV
FFEILYALLR WTPELWWVWA TAVYVAFSVV LTAVAPALIL PLFYKYEPLD RPELNRKIEA
MMAAEGLDVI GVYTWGLAEK TRAANAALAG LGRSRRIILG DTLLEHYDED EILAILAHEL
GHYRGRDTTR LIAAGTVLAA AGFYLADLAL SYLLEQLAIG AVYDIAGLPV LLFCLLLFSV
VSMPLSNAYS RKREFAADAF AARRTENGEA LARALDKLAD QNLADREPPR WIEFLLHSHP
SIGRRIAAIR PPDARN
//
