ID A0A1Y0NBW4_9BURK Unreviewed; 420 AA.
AC A0A1Y0NBW4;
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=Fimbrial protein {ECO:0000313|EMBL:ARV20152.1};
GN Name=pilE1 {ECO:0000313|EMBL:ARV20152.1};
GN ORFNames=AEP_03228 {ECO:0000313|EMBL:ARV20152.1};
OS Curvibacter sp. AEP1-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1844971 {ECO:0000313|EMBL:ARV20152.1, ECO:0000313|Proteomes:UP000196261};
RN [1] {ECO:0000313|EMBL:ARV20152.1, ECO:0000313|Proteomes:UP000196261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AEP1-3 {ECO:0000313|EMBL:ARV20152.1,
RC ECO:0000313|Proteomes:UP000196261};
RA Foret S., Pietschke C., Fraune S.;
RT "Curvibacter sp. AEP1.3.";
RL Submitted (MAY-2016) 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 peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CP015698; ARV20152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0NBW4; -.
DR Proteomes; UP000196261; Chromosome.
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: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; IPR045584; Pilin-like.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF01435; Peptidase_M48; 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:UP000196261};
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 40..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..176
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 420 AA; 46459 MW; A5E1E197FF572622 CRC64;
MILLLSRVNL PNRFQKQTVK MREKMMDELV YPRERVLGKI TLVLGIVAWL LILVGTFGLA
LIYVLLGFIA YVFAQSAWVA AVRGTAVQIT EEQFPDLHAR FKDCCEKLHI DAVPEAYLLN
GNGIFNAFAT RFFGRNFVIL YSDVVDTFEV EPDSINFYIG HELGHIRLKH LTGQLWRLPM
MWLPLLGAAY SRAKEYSCDL HGRACCESAE TAARALIVLG AGPIRVKTTD INAYTQQVVN
AAGFWSSFHE IVNGYPWLTK RVWRIKTPDR TLPKRNPFAY FLGLFVPYGG AAGGGSGFLI
LVAILGVMAA VALPAYQEYT NKAVVSQAWI QSAPTRNQLA AFYGQHQKVP TFREAGLEET
LPDGRRMGIN SESMIVDVPT KAGTLLLVPK VAPDEANGIA WTCEAGEGMK PAALPLSCSN
//
