ID A0A1J6X365_9BACI Unreviewed; 422 AA.
AC A0A1J6X365;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:OIU72569.1};
GN ORFNames=BHE18_08095 {ECO:0000313|EMBL:OIU72569.1};
OS Rossellomorea aquimaris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU72569.1, ECO:0000313|Proteomes:UP000182062};
RN [1] {ECO:0000313|EMBL:OIU72569.1, ECO:0000313|Proteomes:UP000182062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAMM {ECO:0000313|EMBL:OIU72569.1,
RC ECO:0000313|Proteomes:UP000182062};
RA Waghmode S.R., Suryavanshi M.V.;
RT "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT biosurfactant production capacities.";
RL Submitted (SEP-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:OIU72569.1}.
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DR EMBL; MINN01000074; OIU72569.1; -; Genomic_DNA.
DR RefSeq; WP_071618211.1; NZ_MINN01000074.1.
DR AlphaFoldDB; A0A1J6X365; -.
DR OrthoDB; 9781930at2; -.
DR Proteomes; UP000182062; 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:UP000182062};
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..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..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 422 AA; 49124 MW; 4951AF9C1016D8C0 CRC64;
MVRKWAFRAV LGYLLLGLFL YVYLFILADS SLPGSFKGSS ADPATFMNAR QIMLSEEFSK
FKNLLFFLST PYEWLFYFLI LILGVSRGFE KWARGTAKNR FIQTAVYLFW LSLASFIAIF
PLQFISYKIS RTYNISTQNF SMWMKDELTD FWVNYLIMFI IVSVLYGLMK KFKNRWWLAA
WALSVPFTIF MMFIQPVVID PLYNDFYPLK DKALEQKILT LADKAEIPAD HVFEVDMSEK
TNSLNAYVNG VGSNSRIVLW DTTLKQLTDK EILFVMAHEM AHYVEKHIYI GIAIYLVLSF
FGLFLASKLM RGIVANYKDD IKVSNVSSLS SLPLFLLITS MLMFAVSPFS NWISRYQETR
ADRYAIEMTE DKQAAITSFQ KLSKVGLSQV NPPLLVKIFR YGHPTMMERL IMLEQYEKEE
KE
//
