ID A0A1Y0IDT7_9GAMM Unreviewed; 398 AA.
AC A0A1Y0IDT7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:ARU57946.1};
GN ORFNames=OLMES_3926 {ECO:0000313|EMBL:ARU57946.1};
OS Oleiphilus messinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oleiphilaceae; Oleiphilus.
OX NCBI_TaxID=141451 {ECO:0000313|EMBL:ARU57946.1, ECO:0000313|Proteomes:UP000196027};
RN [1] {ECO:0000313|EMBL:ARU57946.1, ECO:0000313|Proteomes:UP000196027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ME102 {ECO:0000313|EMBL:ARU57946.1,
RC ECO:0000313|Proteomes:UP000196027};
RA Kozyavkin S.A., Slesarev A.I., Golyshin P.N., Korzhenkov A.,
RA Golyshina O.N., Toshchakov S.V.;
RT "Genomic insights into alkan degradation activity of Oleiphilus
RT messinensis.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family.
CC {ECO:0000256|ARBA:ARBA00005233}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CP021425; ARU57946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0IDT7; -.
DR KEGG; ome:OLMES_3926; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000196027; Chromosome.
DR GO; GO:0009289; C:pilus; IEA:InterPro.
DR GO; GO:0005886; C:plasma 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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 3.30.700.10; Glycoprotein, Type 4 Pilin; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; Pili subunits; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000196027};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..144
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 398 AA; 44529 MW; AB298C3094A76C60 CRC64;
MNLVYKNEKK LFLIAAILSG IFWFALIVGT FGIALLYLLL GYLFFLFAHS AFITHLKGTG
VKITEKQYPD LHARLVRSCE KVGVTDVPEA YLLRTDFFNA LATRFLGRHF VVLFTDVVDA
LEDQQGAIDF YIGHELGHIH RKHLSWGTFL FPASILPLLG AALRRAEEYT CDRYGVACCE
SEDDIKAALS AIAAGDTRWK SINIDSYVEQ VALTNGFWMS FNELTGDYPW LTKRMATSLS
LARGEEIKHP RRHGLAWFLS IFVPRVGTGG LASLIVTVAI IGILAAVAIP AYKDYTERAR
LSEGYSAAQP IKAGVTDYAV ENRAWPSSLF DLGYEEESVV NHGKNYEIKI YDEGIIGVEV
GDEQYLVLEP SFDYEEGSVS WTCSGQNIEE KFVPRMCK
//