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Database: UniProt
Entry: A0A074M374_ERYLO
LinkDB: A0A074M374_ERYLO
Original site: A0A074M374_ERYLO 
ID   A0A074M374_ERYLO        Unreviewed;       238 AA.
AC   A0A074M374;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KEO88996.1};
GN   ORFNames=EH31_13190 {ECO:0000313|EMBL:KEO88996.1};
OS   Erythrobacter longus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88996.1, ECO:0000313|Proteomes:UP000027647};
RN   [1] {ECO:0000313|EMBL:KEO88996.1, ECO:0000313|Proteomes:UP000027647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88996.1,
RC   ECO:0000313|Proteomes:UP000027647};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL   Submitted (APR-2014) 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: 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEO88996.1}.
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DR   EMBL; JMIW01000006; KEO88996.1; -; Genomic_DNA.
DR   RefSeq; WP_034960769.1; NZ_JMIW01000006.1.
DR   AlphaFoldDB; A0A074M374; -.
DR   STRING; 1044.EH31_13190; -.
DR   eggNOG; COG1994; Bacteria.
DR   OrthoDB; 9800627at2; -.
DR   Proteomes; UP000027647; Unassembled WGS sequence.
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 YWHC-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:UP000027647};
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        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          145..199
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   238 AA;  25114 MW;  5B2E67E8CC78AA8D CRC64;
     MFDTLSFAAV FIPCLVIAIV FHEVAHGLAA KALGDPTASE RGRLTLNPIR HVDPIGTLLV
     PGGLLLMGAP AFGWAKPVPV NKWRLANPRF GMMAVAAAGP AMNFALAFVG AVAFGIIGTP
     GAGWAEGGAG FPMLIAPDGT TLPVATGLYL FMLINVFLGM FNLLPIPPFD GSHILGGLLP
     KPLRKHWEKL QRFGMVLILG VIGFSWVFGT GWLEVTVLPL VAAVMSFYEG VANWVALA
//
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