ID C7R802_KANKD Unreviewed; 422 AA.
AC C7R802;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=PepB aminopeptidase {ECO:0000313|EMBL:ACV25784.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:ACV25784.1};
GN OrderedLocusNames=Kkor_0363 {ECO:0000313|EMBL:ACV25784.1};
OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV25784.1, ECO:0000313|Proteomes:UP000001231};
RN [1] {ECO:0000313|EMBL:ACV25784.1, ECO:0000313|Proteomes:UP000001231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC {ECO:0000313|Proteomes:UP000001231};
RX PubMed=21304661; DOI=10.4056/sigs.36635;
RA Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL Stand. Genomic Sci. 1:226-233(2009).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; CP001707; ACV25784.1; -; Genomic_DNA.
DR RefSeq; WP_012800299.1; NC_013166.1.
DR AlphaFoldDB; C7R802; -.
DR STRING; 523791.Kkor_0363; -.
DR MEROPS; M17.004; -.
DR KEGG; kko:Kkor_0363; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_7_1_6; -.
DR InParanoid; C7R802; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000001231; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ACV25784.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACV25784.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001231}.
FT DOMAIN 268..275
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 422 AA; 44947 MW; 69D7A9BE9A1DC24B CRC64;
MTLKVLLSKD SAPAHWGEGA LLSYKEDAVT IHAEGADLVQ MAARKLVSQG LSFFALQGDW
ELEQQWAFFQ GSYEPKIDVQ IDFADLSDDD NKELEARIQT SRWMRSIVNE TPEVLAPQVL
AQEAADFIQS LAPDNVRYQI VSGQDLEKQG HVGTWEVGRG STRPPAILKL EFDPKNDSSA
PVAALVGKGI TFDSGGYSIK QSAGMVHMKA DMGGAATVTA GLALAILRGL DKPVHLYLCC
AENLISGHAY KLGDIITYPN GISVEIHNTD AEGRLVLADG LLLAGQTGAP LIIDAATLTG
AAVTAVGEDY NAVFALDDDE RNDYLNVAQS ENERHWPLPL EPFHAAKCPS NFADTANSRA
VKGGGPGGAS NAAGFLSRFV PNDGKGWIHV DLAGAYNDSP TAYFAAGGTG HGFRTIAAKL
LK
//
