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Database: UniProt
Entry: B2GGK4_KOCRD
LinkDB: B2GGK4_KOCRD
Original site: B2GGK4_KOCRD 
ID   B2GGK4_KOCRD            Unreviewed;       464 AA.
AC   B2GGK4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   22-NOV-2017, entry version 58.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=KRH_19730 {ECO:0000313|EMBL:BAG30320.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 /
OS   DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30320.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30320.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N.,
RA   Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria
RT   rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; AP009152; BAG30320.1; -; Genomic_DNA.
DR   RefSeq; WP_012399041.1; NC_010617.1.
DR   ProteinModelPortal; B2GGK4; -.
DR   STRING; 378753.KRH_19730; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; BAG30320; BAG30320; KRH_19730.
DR   KEGG; krh:KRH_19730; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; KRHI378753:GJ8F-2025-MONOMER; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008838};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:BAG30320.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   464 AA;  48386 MW;  2E0767F8D4168B14 CRC64;
     MTHTTEKPGT GPADIPAHAA FARDLGEFVT ASPSSYHAVA TAAAALEAAG FTALDEAQPW
     EIGPGRWYTV RDGALIAWVS PSGAAPGTGY RILGAHTDSP GFKLKPRPTT VTHRWYQAGV
     EVYGGALLNS WLDRDLRFAG RLVVSGADGA PRTVLTSTGP VARIPQLAIH LDRSTNDGLA
     LDRQRHTQPV WGVGDAQDAD VLAVLAAAVH APTAGSVTPN GGGTSEGNAL TVDPADIMGY
     DITVADTQAP ELIGAQQNLL ASGRLDNLTT VHAGLRALVE HAEELESAPQ VSVLAAFDHE
     EVGSATRSGA AGPFLEDVLV RIGAARGDST DEHRRALAES VCLSSDAGHL VHPNYPGHHD
     PVNTPEPGRG PLLKINAQQR YTTDAVGAAV WAHACDVAGV DYQEFVSNNG VPCGSTIGPI
     TATRLGIRTL DVGVGLLSMH SARELVHTGD LFALHRAIGG FWRG
//
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