ID A0A1H9VMM1_9BACI Unreviewed; 441 AA.
AC A0A1H9VMM1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:SES22986.1};
GN ORFNames=SAMN05518872_10623 {ECO:0000313|EMBL:SES22986.1};
OS Psychrobacillus sp. OK032.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1884358 {ECO:0000313|EMBL:SES22986.1, ECO:0000313|Proteomes:UP000199084};
RN [1] {ECO:0000313|EMBL:SES22986.1, ECO:0000313|Proteomes:UP000199084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK032 {ECO:0000313|EMBL:SES22986.1,
RC ECO:0000313|Proteomes:UP000199084};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; FOGY01000006; SES22986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9VMM1; -.
DR STRING; 1884358.SAMN05518872_10623; -.
DR Proteomes; UP000199084; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 CDD; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01435; Peptidase_M48; 2.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SES22986.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..154
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT DOMAIN 158..241
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 320..352
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 353..385
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 441 AA; 49186 MW; 98956A501C9C32D4 CRC64;
MSPRELMSNR EMPYFVISLI FSLLLYILAI VSLFGIAILL VLFAFLLYAN MIMLGSIRGN
GVRISEKQFP DVYERVLSLS TEMNIKKVPD VFVIHSEGAF NAFATRFLGR NMVVIYSEVF
ELARERGEAE LDFIIAHELS HVKRRHVWKN ILIMPAQFIP FLSQAYSRSC EYTCDREAAY
YIQNGEAAKR ALTILGIGKN LYKEVNEDAY LEQIHTESNV AVWLSEVLSS HPLLPKRIQA
VGNFMKIDGT PTYYSNSTKI ALGIGAFIGI FFVCYLAVIA LLTAGTFTYA SLFSGSVFNE
LSSGDELSSE EDFLSSDYSL TLTPLMEAVS NGDDRMVREL LSTGAELEET DSENTTALHY
AIYGDNITMA ELLLVRGANP NTVDDYTNAL TAALETQNFE MASLLYAHGA NPTMKDPQGY
SALDMLGVNS EEDFINIINN N
//
