ID A0A265QBP5_9FIRM Unreviewed; 409 AA.
AC A0A265QBP5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptidase M48 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CIW83_01720 {ECO:0000313|EMBL:OZV13686.1};
OS Tissierella sp. P1.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1280483 {ECO:0000313|EMBL:OZV13686.1, ECO:0000313|Proteomes:UP000216906};
RN [1] {ECO:0000313|EMBL:OZV13686.1, ECO:0000313|Proteomes:UP000216906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:OZV13686.1,
RC ECO:0000313|Proteomes:UP000216906};
RA Bukhtiyarova P.A., Antsiferov D.V., Avakyan M.R., Frank Y.A., Ikkert O.P.,
RA Pimenov N.V., Brasseur G., Tuovinen O.H., Karnachuk O.V.;
RT "Isolation and Characterization of an Anaerobic Sulfidogenic Tissierella
RT from Cu-bearing Coins.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:OZV13686.1}.
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DR EMBL; NPMN01000002; OZV13686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265QBP5; -.
DR OrthoDB; 9781930at2; -.
DR Proteomes; UP000216906; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000216906};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..195
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 200..401
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 409 AA; 48269 MW; 727692F6895CC048 CRC64;
MNSKLKLIII LFFIFLLAFI GGVLVSEYIN MNKIRTEYPD LPENAYNLRK DSLKVWAIRL
VLQFLIPLLF LTSRLSYRIR YYVDNNRSLF FTGLLYGIIF FTIMFLVNLP LDYYSSFYLK
HKYGLSNQTF GRWIEVALKS FLINDLVISF FIFIPFYLMY RSPKIWWLQL SFLAIPVIIF
MVFISPFVID PIFNKYTSME NEKLGRQITE LLQEANIQDA KIYKVDKSRD TKTMNAYMTG
IFHSKRIVLW DTTINNLEEK EVLSITAHEI GHYVKGHIWK NIIFSSLGTV LLLFLVYITA
TWILNLSNGT FGIRKLHDIA AIPLLILVLN FYSFIGSPIT NYLSREMEIE ADTYEIMLTR
DRESAISAME KLYKESLGLP RPSNIFKIWY YTHPTLEERV DFYRNYPLD
//
