ID A0A2Z6IAX8_9BURK Unreviewed; 219 AA.
AC A0A2Z6IAX8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:BBF22747.1};
GN ORFNames=SUTMEG_06380 {ECO:0000313|EMBL:BBF22747.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF22747.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF22747.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF22747.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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; AP018786; BBF22747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6IAX8; -.
DR KEGG; sutt:SUTMEG_06380; -.
DR Proteomes; UP000271003; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06158; S2P-M50_like_1; 1.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR044537; S2P-M50-like.
DR PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000271003};
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 62..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..196
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 219 AA; 23322 MW; 026237A1F9903BA8 CRC64;
MMSSFASAVQ TVCVYAIPLI FAITLHEAAH GWAAARLGDR TALYLGRVTA NPVPHIDPVG
TIAVPGALLL LSALTGGGGL LFGWAKPVPI NTRNFRRPLR DMMLTAAAGP AANALQMVFW
LFLLKGLVGL GIYEKFVVSV CTAGISTNLM LMAFNLIPIP PLDGGRILRG LLPGRSGYWL
DRAEPYGFVI LVVLMMSGAL SYFIAPFLWA GQAIVNAVL
//
