ID F0FFA7_STRSA Unreviewed; 353 AA.
AC F0FFA7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Creatinase {ECO:0000313|EMBL:EGC22172.1};
DE EC=3.4.13.9 {ECO:0000313|EMBL:EGC22172.1};
GN Name=pepQ2 {ECO:0000313|EMBL:EGC22172.1};
GN ORFNames=HMPREF9388_1389 {ECO:0000313|EMBL:EGC22172.1};
OS Streptococcus sanguinis SK353.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC22172.1, ECO:0000313|Proteomes:UP000004185};
RN [1] {ECO:0000313|EMBL:EGC22172.1, ECO:0000313|Proteomes:UP000004185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK353 {ECO:0000313|EMBL:EGC22172.1,
RC ECO:0000313|Proteomes:UP000004185};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGC22172.1}.
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DR EMBL; AEWY01000007; EGC22172.1; -; Genomic_DNA.
DR RefSeq; WP_002898282.1; NZ_GL872307.1.
DR AlphaFoldDB; F0FFA7; -.
DR PATRIC; fig|888815.3.peg.1363; -.
DR HOGENOM; CLU_017266_4_0_9; -.
DR Proteomes; UP000004185; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
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 Dipeptidase {ECO:0000313|EMBL:EGC22172.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGC22172.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:EGC22172.1}.
FT DOMAIN 4..127
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 135..337
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 353 AA; 39386 MW; 8A71CF93E6AD1A7C CRC64;
MLSRVEKFEA ALAQTDCDAV LVTNLKNIYY LTGFSGTEAT VFISKNRRIF LTDARYTLIA
KGVVQGFDIV ETRDAIGEIV KIIADDKLQK IGFDDEISYA YFKMLESAFS AYELVPMTAF
IENLRMIKDE QEIATIRKAC QISDQAFLDV LDFIKPGETT ELAVMNFLDA RMRQLGASGA
SFDFIIASGY RSAMPHGVAS DKVIQKGETL TMDFGCYYNH YVSDMTRTVH VGQVTDEERE
IYDIVLRSNQ ALIEAAKAGL SRIDFDRIPR HIINDAGYGP YFSHGIGHGI GLDIHEIPYF
GKSEEPIEAG MVLTDEPGIY LDGKYGVRIE DDLLITETGC EVLTLAPKEL IVI
//