ID K8E5L4_CARML Unreviewed; 412 AA.
AC K8E5L4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Aminopeptidase pepS {ECO:0000313|EMBL:CCO12025.2};
DE EC=3.4.11.- {ECO:0000313|EMBL:CCO12025.2};
GN Name=pepS {ECO:0000313|EMBL:CCO12025.2};
GN ORFNames=BN424_2586 {ECO:0000313|EMBL:CCO12025.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO12025.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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DR EMBL; HE999757; CCO12025.2; -; Genomic_DNA.
DR RefSeq; WP_015077085.1; NC_019425.2.
DR AlphaFoldDB; K8E5L4; -.
DR STRING; 1234679.BN424_2586; -.
DR MEROPS; M29.004; -.
DR KEGG; cml:BN424_2586; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_054346_1_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000000212; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CCO12025.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCO12025.2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000212}.
SQ SEQUENCE 412 AA; 45065 MW; C81ADFD6F23BBA31 CRC64;
MVLPNFQENL QKYADLIVST GVNVDKGQTV VLQIDVEQAP LARLITRAAY KKGATEVIVK
WTDDEINREI FLGTPEERLT DIPQYKIDES LDQLEKNASR ISVRSADPDA LSGVDSTKVA
AYQSAAGKAL KAMRIATQSN KVSWTVVAAS GEKWAAKVFP NLATSEEQVD ALWDQIFKTT
RIYTPDPVAA WNAHDQLLES KADELNKEQF DALHYTAPGT DFTIGLPKGH RWEGAGSFNA
RGEKFMANMP TEEVFTAPDA NRADGVIKST KPLSYAGTTI LDMTFTFKDG QVVDVTAKEG
EDVLKHLIAT DNGSKRLGEV ALVPDPSPIS QSGIVFYNTL FDENASNHLA LGSAYAFSLE
GGTEMTEEEL IAAGLNRSDV HVDFMVGSNE MDVDGIRLDG TRVPIFRKGN WA
//
