ID I9WDU8_HELPX Unreviewed; 357 AA.
AC I9WDU8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Metallopeptidase M24 family protein {ECO:0000313|EMBL:EJC04152.1};
GN ORFNames=HPHPP4_0628 {ECO:0000313|EMBL:EJC04152.1};
OS Helicobacter pylori Hp P-4.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992075 {ECO:0000313|EMBL:EJC04152.1, ECO:0000313|Proteomes:UP000004561};
RN [1] {ECO:0000313|EMBL:EJC04152.1, ECO:0000313|Proteomes:UP000004561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-4 {ECO:0000313|EMBL:EJC04152.1,
RC ECO:0000313|Proteomes:UP000004561};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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:EJC04152.1}.
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DR EMBL; AKPL01000001; EJC04152.1; -; Genomic_DNA.
DR RefSeq; WP_001214526.1; NZ_AKPL01000001.1.
DR AlphaFoldDB; I9WDU8; -.
DR PATRIC; fig|992075.3.peg.613; -.
DR Proteomes; UP000004561; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 29..107
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 131..350
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 357 AA; 40850 MW; 428C034A6DE4B0AD CRC64;
MRGLERDSHF TLNENAMFFE CAYSCDNALF LQLEDRSFFI TDSRYTQEAK ESIQPKKGVL
AEVIESSDLV QSAIDLIAKS SVKKLFFDPN QVNLQTYKRL DSAIGNKVIL EGVPSYHRQK
RIIKNEHEIQ LLKKSQALNV EAFENFAEYV KKIFDEKESL SERYLQHKVK DFLTKEGVYD
LSFEPILALN ANASKPHALP SAKDFLKAEH SILLDMGIKY ERYCSDRTRT AFFDPKDFVF
KREQSFKDKE RQKIYDIVKE AQEKAISGIR AGMTGKEADS LARGVISDYG YGQYFTHSTG
HGIGLDIHEL PYISSRSETI LEEGMVFSIE PGIYIPGFFG VRIEDLVVIK NSRAELL
//