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Database: UniProt
Entry: A0A0M4LGV3_9GAMM
LinkDB: A0A0M4LGV3_9GAMM
Original site: A0A0M4LGV3_9GAMM 
ID   A0A0M4LGV3_9GAMM        Unreviewed;       414 AA.
AC   A0A0M4LGV3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:ALE01964.1};
GN   ORFNames=W908_05010 {ECO:0000313|EMBL:ALE01964.1};
OS   Candidatus Pseudothioglobus singularis PS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX   NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01964.1, ECO:0000313|Proteomes:UP000068905};
RN   [1] {ECO:0000313|EMBL:ALE01964.1, ECO:0000313|Proteomes:UP000068905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS1 {ECO:0000313|EMBL:ALE01964.1,
RC   ECO:0000313|Proteomes:UP000068905};
RX   PubMed=26494659;
RA   Marshall K.T., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT   Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01155-e01115(2015).
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}.
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DR   EMBL; CP006911; ALE01964.1; -; Genomic_DNA.
DR   RefSeq; WP_053820178.1; NZ_CP006911.1.
DR   AlphaFoldDB; A0A0M4LGV3; -.
DR   STRING; 1125411.W908_05010; -.
DR   KEGG; tsn:W908_05010; -.
DR   OrthoDB; 9781930at2; -.
DR   Proteomes; UP000068905; Chromosome.
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:UP000068905};
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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..208
FT                   /note="CAAX prenyl protease 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16491"
FT   DOMAIN          212..413
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   ACT_SITE        363
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ   SEQUENCE   414 AA;  47345 MW;  F7D5CB449D0EE9F5 CRC64;
     MEFNFFTFIF LFAILTSVLA LLYLNFRQDK AIDNSFDAVP DGFSETIKLE DHQKAGKYTK
     AKLLLNHFEI IFSTMVLLVW TLGGAMNWID GYWSQRVNDP VLMGTFFVLS IMLIASFIDL
     PFSIYRNFVL EQKFGFNRMT VGTFAGDLIK EIILSLVLVL PLIYAILYLM NIESIGNYWW
     IYVWVIISLF SLIMMWVYPS FIAPIFNKFN PLVNESLKTR ITSLLERTGF GSDGIYVMDG
     SKRSSHGNAY FTGIGKNKRI VFFDTLLNGM EDKEIEAILA HELGHFHHKH TRQRMISSFI
     FSFISLALLG YLINQTWFFN GLGISEPSSH AALVLFSLAL PVFSFFITPI SNLVSRKHEF
     QADAFAASHT DAKDLISSLI KLYKENSSSL SPDRYYSAFH DSHPSAVLRI EKLL
//
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