ID A0A1H8HP05_9BACI Unreviewed; 418 AA.
AC A0A1H8HP05;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN04488134_101391 {ECO:0000313|EMBL:SEN57418.1};
OS Amphibacillus marinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=872970 {ECO:0000313|EMBL:SEN57418.1, ECO:0000313|Proteomes:UP000199300};
RN [1] {ECO:0000313|EMBL:SEN57418.1, ECO:0000313|Proteomes:UP000199300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10434 {ECO:0000313|EMBL:SEN57418.1,
RC ECO:0000313|Proteomes:UP000199300};
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 ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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DR EMBL; FODJ01000001; SEN57418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8HP05; -.
DR STRING; 872970.SAMN04488134_101391; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000199300; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SEN57418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199300};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 391..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 184..257
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 418 AA; 46776 MW; 2E2BC6BD53158C65 CRC64;
MNTIVAFILM FGLLVFVHEF GHFIVAKKTG MLVREFAIGF GPKIFSIKRA ETLYTIRILP
MGGYVRVAGE DPEIVELKPG QHIGLKYNKQ GQVNKIIVNN KDKHPTAEVI EVEQADLTHQ
LQIKGMLIGE EEVKVYQIAV DADYVMNESE TRIAPFDRQF AAKTKLQRSA QLFAGPLMNF
ILTALLFFAL AAFSGIPVED ARLGEIAPNS PAEQAGLQPG DQITQIDQVE INSWLDFQRY
VSERPNQELT INYLRDGEAD KLTIVPTSEQ LDDSEVGRIG VRQYMERSVT RAIPYSLTQT
YEWSKLILVN LGMLVTGQFS VDMLSGPVGI YDFTDQVVQT GFWNFVQWTA ALSVNLGIIN
LLPLPALDGG RLLFVGIEAI RGKPISPEKE GLVHFVGFAL LMLLMVIVTW NDIQRLFL
//
