ID C5CB99_MICLC Unreviewed; 532 AA.
AC C5CB99;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:ACS31022.1, ECO:0000313|EMBL:SQG47445.1};
DE EC=3.4.11.9 {ECO:0000313|EMBL:SQG47445.1};
GN Name=pepPI {ECO:0000313|EMBL:SQG47445.1};
GN OrderedLocusNames=Mlut_15300 {ECO:0000313|EMBL:ACS31022.1};
GN ORFNames=NCTC2665_00205 {ECO:0000313|EMBL:SQG47445.1};
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS31022.1, ECO:0000313|Proteomes:UP000000738};
RN [1] {ECO:0000313|EMBL:ACS31022.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS31022.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT "Complete sequence of Micrococcus luteus NCTC 2665.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX PubMed=19948807; DOI=10.1128/JB.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [3] {ECO:0000313|EMBL:SQG47445.1, ECO:0000313|Proteomes:UP000248985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG47445.1,
RC ECO:0000313|Proteomes:UP000248985};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; CP001628; ACS31022.1; -; Genomic_DNA.
DR EMBL; LS483396; SQG47445.1; -; Genomic_DNA.
DR RefSeq; WP_010080559.1; NZ_LS483396.1.
DR AlphaFoldDB; C5CB99; -.
DR STRING; 465515.Mlut_15300; -.
DR MEROPS; M24.033; -.
DR EnsemblBacteria; ACS31022; ACS31022; Mlut_15300.
DR KEGG; mlu:Mlut_15300; -.
DR PATRIC; fig|465515.4.peg.1467; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_1_0_11; -.
DR Proteomes; UP000000738; Chromosome.
DR Proteomes; UP000248985; Chromosome 1.
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:ACS31022.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SQG47445.1};
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:UP000000738}.
FT DOMAIN 70..225
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 57437 MW; 70943C19CC3BB811 CRC64;
MTDAAQHPAQ TTPDQPAAAP EAGADGTGAV NPQPLAERVD NRSQRPASNA FRDFMASDWA
PSSQALPDPD ASAPYAARRR AAVSARFPGE RIVVPAGRLK VRSNDTDYRF RAHSAFAHLT
GLGVDHEPDA VLVLEPTDPG AGDDGTDHTA TLYFRPLAGR DTEQFYADSR SGEFWIGPRP
TLAGLAARTG LRTAGLEELE SAITKNVAAD GTAVRLLAET DQDVDALLAA VRTEAGVDLA
AAAEADAQTA EFLSELRLVK DAWEVERMRA SVAATIAGFE DVVRALPRAV GHDRGERVVE
GAFFARARLE GNDLGYDTIA ASGNNATILH WIRNTGAVRP GELLLLDAGV EDDSLYTADI
TRTLPVSGTF TDVQRRIYQA VLDAADAAFA IVRPGIRFRE LHAEAMRVLV DRLDGWGLLP
VSAEVALSDE GQHHRRWMPH GTSHHLGLDV HDCAQAKREL YLDGVLEPGM VFTIEPGLYF
KEEDLAVPED YRGIGVRIED DILVTEDGAE NLSAVLPRTP DEIEAWMARL QA
//
