ID K0J3A0_AMPXN Unreviewed; 418 AA.
AC K0J3A0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN OrderedLocusNames=AXY_14650 {ECO:0000313|EMBL:BAM47597.1};
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47597.1, ECO:0000313|Proteomes:UP000006294};
RN [1] {ECO:0000313|EMBL:BAM47597.1, ECO:0000313|Proteomes:UP000006294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC Ep01 {ECO:0000313|Proteomes:UP000006294};
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) 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; AP012050; BAM47597.1; -; Genomic_DNA.
DR RefSeq; WP_015010196.1; NC_018704.1.
DR AlphaFoldDB; K0J3A0; -.
DR STRING; 698758.AXY_14650; -.
DR MEROPS; M50.011; -.
DR KEGG; axl:AXY_14650; -.
DR PATRIC; fig|698758.3.peg.1461; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000006294; Chromosome.
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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 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}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006294};
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 191..268
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 418 AA; 46564 MW; 607C82431E4C5611 CRC64;
MNTIVAFILM FGLLVFVHEF GHFIFAKRAG MLVREFAIGF GPKIFSVKKG ETLYTIRILP
MGGYVRVAGE DPEIVDLKPG QHIGLIFNQD NKVQKIVINH KAKYPQAHVI EVERADLDHE
LIIIGSLVGE EDIKTYHVAE NAEYIMDEVA TQIAPYNRQF ASKTKRQRAM QLFAGPLMNF
VLTAVLFFFM GSIQGIPVDE AILGEIQPNS PADIAGFQSG DEVISVQGKS ISQWSEFQQF
IRENPEQELL MTVNRSGQQI EITVTPGANE EGELTIGRIG VLPYIEKSPL RAVPYSIKQT
YEWSKLIVIN VGMLVSGQFS LDMLGGPVAI YDATDQMVQS GFWTLIHWTA ALSVNLGVIN
LLPLPALDGG RLLFIGIEAI RGKPISTEKE GLVHFIGFAL LMLLMIIVTW NDIQRLFM
//
