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Database: UniProt
Entry: A0A3R5VAG1_9CLOT
LinkDB: A0A3R5VAG1_9CLOT
Original site: A0A3R5VAG1_9CLOT 
ID   A0A3R5VAG1_9CLOT        Unreviewed;       211 AA.
AC   A0A3R5VAG1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Site-2 protease family protein {ECO:0000313|EMBL:QAA33871.1};
GN   ORFNames=C1I91_20790 {ECO:0000313|EMBL:QAA33871.1};
OS   Clostridium manihotivorum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2320868 {ECO:0000313|EMBL:QAA33871.1, ECO:0000313|Proteomes:UP000286268};
RN   [1] {ECO:0000313|EMBL:QAA33871.1, ECO:0000313|Proteomes:UP000286268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT4 {ECO:0000313|EMBL:QAA33871.1,
RC   ECO:0000313|Proteomes:UP000286268};
RA   Tachaapaikoon C., Sutheeworapong S., Jenjaroenpun P., Wongsurawat T.,
RA   Nookeaw I., Cheawchanlertfa P., Kosugi A., Cheevadhanarak S.,
RA   Ratanakhanokchai K.;
RT   "Genome Sequencing and Assembly of Anaerobacter polyendosporus strain
RT   CT4.";
RL   Submitted (JAN-2018) 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}.
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DR   EMBL; CP025746; QAA33871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R5VAG1; -.
DR   KEGG; cmah:C1I91_20790; -.
DR   OrthoDB; 9800627at2; -.
DR   Proteomes; UP000286268; 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, ECO:0000313|EMBL:QAA33871.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286268};
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        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..171
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   211 AA;  23653 MW;  E20928620C516C81 CRC64;
     MREKLLDIII MIPAILIGFT FHEYAHAKVA DIVGDKTPRF QGRLTLNPLA HIDPIGFLLI
     LVMKFGWAKP VQVNRRNFKN GYKDDLKVTI AGPLANLFVA ILFSVVFGLA FRFYFVDNYT
     QLSKIVIDIL NAIIVININL FVFNLLPLPG LDGFGILEDL FPSFFSRISD SLYRYQFIII
     ALIAFGGARY LSIPTGAIQK LCGKLITAIA L
//
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