ID I4D8X9_DESAJ Unreviewed; 353 AA.
AC I4D8X9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:AFM42253.1};
GN OrderedLocusNames=Desaci_3358 {ECO:0000313|EMBL:AFM42253.1};
OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM42253.1, ECO:0000313|Proteomes:UP000002892};
RN [1] {ECO:0000313|EMBL:AFM42253.1, ECO:0000313|Proteomes:UP000002892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22704 / JCM 16185 / SJ4
RC {ECO:0000313|Proteomes:UP000002892};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; CP003639; AFM42253.1; -; Genomic_DNA.
DR AlphaFoldDB; I4D8X9; -.
DR STRING; 646529.Desaci_3358; -.
DR MEROPS; M24.008; -.
DR KEGG; dai:Desaci_3358; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_9; -.
DR Proteomes; UP000002892; Chromosome.
DR GO; GO:0004177; F:aminopeptidase 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 SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AFM42253.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:AFM42253.1}.
FT DOMAIN 3..126
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 134..336
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 353 AA; 39282 MW; 338869EE4F1F9843 CRC64;
MTRLERMRQR MREESIDTFV VLRPENGRYL SGFSGGEASL IITLDRSYLL TDFRYIEQAK
EQSPDFEIVK TGHDHFMMMA EMGLQSRRVG FEGDFITFAD YEKLKQSFTQ AQLISMPGLV
TDLRSVKDDQ EIPLIRQAVQ IADKAFSEVL KSLEIGQTEE EVGLNLEFSM RRLGASGGSF
EFIVASGIRG AMPHGTASPK KIKDGEFLTM DFGAIYRGYC SDITRTIFLG DPSEKQRELY
ALVLNAQRAG IAAVAPGRTG KEVDAAARKI IEEAGYGENF GHGLGHSVGL AIHEGPNFNQ
REERVLEPGM VLTVEPGIYI PDWGGIRIED MVLVTEDGCE VLTQAPKELI LLN
//
