ID A0A1S1RBD5_9ACTN Unreviewed; 468 AA.
AC A0A1S1RBD5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OHV44113.1};
GN ORFNames=CC117_10670 {ECO:0000313|EMBL:OHV44113.1};
OS Parafrankia colletiae.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV44113.1, ECO:0000313|Proteomes:UP000179627};
RN [1] {ECO:0000313|Proteomes:UP000179627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA Hurst S.;
RT "Sequence Frankia sp. strain CcI1.17.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, 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:OHV44113.1}.
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DR EMBL; MBLM01000025; OHV44113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1RBD5; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000179627; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 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; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 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:OHV44113.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000179627}.
FT DOMAIN 16..159
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 468 AA; 51161 MW; 657F367F28E81BAD CRC64;
MASGWAPVDD TVAPRDECAP YTTKRRSLLA TRFPADTLVV PSGGIHVRAN DTDYPFRPGS
DFFWLTGCHE PDAVLILHPN AAGDHDAVLY LADRSDRSSS AFYTDRRYGE LWVGPRPGVR
ETTAALDVEC RPLPELPEAL ARLAPARTRV LRGLDARVDR AVSRWAPTTS SADRDAVLAQ
TLSELRLVKD DFEIARLDEA VAATIVGFTE CMTEFERAAA LPNGERWLEG TFWRRARVDG
NDVGYGSIVA CGPHSTTLHW VRDDGPVRPG DLALLDMGVE GRSLYTADLT RTLPVGGRFS
PLQRQVHDVV YQAQQAGIAA VRPGATFLDP HRAAMRVIAA ALHDWGLLPV TPEESLSEDP
KAPGAGLHRR YTLHSTSHML GLDVHDCAQA RDETYRDAAL EAGMVLTVEP GLYFQPDDLT
VPPELRGIGV RIEDDILVTS DGSRNMSAGL VRSADEVERW MAGEAGRC
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