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Database: UniProt
Entry: X2H8E3_9NEIS
LinkDB: X2H8E3_9NEIS
Original site: X2H8E3_9NEIS 
ID   X2H8E3_9NEIS            Unreviewed;       446 AA.
AC   X2H8E3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SALWKB2_0046 {ECO:0000313|EMBL:AHN27428.1};
OS   Snodgrassella alvi wkB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN27428.1, ECO:0000313|Proteomes:UP000019668};
RN   [1] {ECO:0000313|EMBL:AHN27428.1, ECO:0000313|Proteomes:UP000019668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WkB2 {ECO:0000313|EMBL:AHN27428.1};
RX   PubMed=25053814;
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "Genomics and host specialization of honey bee and bumble bee gut
RT   symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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; CP007446; AHN27428.1; -; Genomic_DNA.
DR   RefSeq; WP_025329701.1; NZ_CP091515.1.
DR   AlphaFoldDB; X2H8E3; -.
DR   STRING; 1196094.SALWKB2_0046; -.
DR   GeneID; 32537269; -.
DR   KEGG; salv:SALWKB2_0046; -.
DR   PATRIC; fig|1196094.4.peg.46; -.
DR   HOGENOM; CLU_025778_0_2_4; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000019668; 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; 2.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 2.
DR   Gene3D; 2.30.42.10; -; 2.
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; PF00595; PDZ; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   PROSITE; PS50106; PDZ; 2.
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:AHN27428.1};
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        94..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        420..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          128..183
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          219..249
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   446 AA;  48498 MW;  6C2FFC6A89F86A38 CRC64;
     MLLTIFAFIV AILLLVSLHE LGHLIVARWC GVKVLRFSIG FGKPFFCLKR GNIEWCLAPI
     PLGGYVKMVD TREGDVSEAD LPYAFDKQHP LKRIAIVVAG PLTNLILAVL LYAASFSIGG
     ITQIRPWVGM VEPATVAADA GFQQGDRINS VNGQAVTDWT DAQAKIMLNL DSGKVQVDVI
     NAAGQPQQRQ LNIAGTDAAA NVAKTGYLGI APFKVINQIG MVIPDSVAAK AGLRTGDILL
     TINGRKLTGW QDWVDSIRAS AGAKLDISYQ RSGQILQTSL RPESVLEKGA IIGQVGVGAM
     RDKTWDAQIR QHYQPGFFES ARLAMQRTWD YITLTLSMFA KLLTGQASLH YLSGPLTIAD
     VAGKTAAMGW QSYTEFLALV SVSLGVLNLL PVPVLDGGHL LYYAIEWIRG RPLSLRIQEM
     GLRFGIAAML MLMLVAFFND ITRLFG
//
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