ID A0A150KPV7_9BACI Unreviewed; 419 AA.
AC A0A150KPV7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYC97182.1};
GN ORFNames=B4102_0837 {ECO:0000313|EMBL:KYC97182.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYC97182.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYC97182.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYC97182.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) 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:KYC97182.1}.
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DR EMBL; LQYN01000086; KYC97182.1; -; Genomic_DNA.
DR RefSeq; WP_066233979.1; NZ_NAZD01000316.1.
DR AlphaFoldDB; A0A150KPV7; -.
DR STRING; 46224.B4102_0837; -.
DR PATRIC; fig|46224.3.peg.4246; -.
DR OrthoDB; 9781930at2; -.
DR Proteomes; UP000075666; 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:UP000075666};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..204
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 208..415
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 419 AA; 49172 MW; 81E32FBFA010889A CRC64;
MLRKWTFRAV IAYLLFGIAV YVYLFYLAGS TVPDHLKGTS VDPATFLNSR EIMLSEEYSK
IRNLLYFIST PYEWLFYFLI LIFGISKGFE RWAESTSRLH IIQSAIYLFL LSVISFVVTF
PLSYISYRFS KAYNISTQTF TLWMKDEVID FWVNFIEMFI IVTVLYWLMK RFKRRWWVPA
WLLSIPFMIF MMFIQPVVID PLYNDFYPLK NKDLETKILA LAEKANIPAE HVYEVNMSEK
TNALNAYVTG IGSNARIVLW DTTLEQLNEK EILFIMAHEM GHYVEKHIYF GIAGYIILTG
IGLWITAWVM NRLVRKKGAE LKITAVSSLS SLPLFLLITS VLLFAASPIT NWVSRYEEMR
ADRYGMEMTN DKKAAVQTFH DLTKSGLSQV NPPYLVKIFR YDHPTMLERI RMVEEFKKK
//
