ID Q1IU23_KORVE Unreviewed; 503 AA.
AC Q1IU23;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Peptidase M16-like protein {ECO:0000313|EMBL:ABF39627.1};
GN OrderedLocusNames=Acid345_0622 {ECO:0000313|EMBL:ABF39627.1};
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Koribacter.
OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF39627.1, ECO:0000313|Proteomes:UP000002432};
RN [1] {ECO:0000313|EMBL:ABF39627.1, ECO:0000313|Proteomes:UP000002432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF39627.1,
RC ECO:0000313|Proteomes:UP000002432};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP000360; ABF39627.1; -; Genomic_DNA.
DR RefSeq; WP_011521429.1; NC_008009.1.
DR AlphaFoldDB; Q1IU23; -.
DR STRING; 204669.Acid345_0622; -.
DR EnsemblBacteria; ABF39627; ABF39627; Acid345_0622.
DR KEGG; aba:Acid345_0622; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_2_0; -.
DR OrthoDB; 9762027at2; -.
DR Proteomes; UP000002432; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004191326"
FT DOMAIN 49..87
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 250..426
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 503 AA; 56578 MW; 1B44784D620B90D0 CRC64;
MKCPVAKLVF ALLLLSSFLA AQDEASFEKR VTVKKLPNGL TIVICERHEA PVFSFYTVVD
AGSSQDPRGR TGLAHMFEHM AFKGTPTIGT TDWPAEKAAL AKVETAYTAY IDERDKRVGR
DDAKVASLQK AWKDTIADAN KYVIPNQFGQ IVESAGGEGM NASTSWDSTD YLYSMPVNKF
ELWAYLESER FLHPVMREFY KERDVVVEER RMRTESSPVG RLIEQFTAAS FTASPYHRPT
VGYYSDLQTF SATDAEKFFH TYYIPSNMVI GLVGDLDPAK VMPILEKYFA RIPSGPKPID
ETSVEPPQNS ERIVKLTDAS QPYYLEGYHR PDYMNADDAV YDVITDLLSD GRTSRLYRSL
VRDKKIALAA AGFSGFPGVK YAHLFVFYAL PTQGHTTQEV ADAIHVEINK LKTTDVTDEE
LQMIKTREKA GLIRRLGSNE GLANELAVYQ TRYGDWHELF KSVDRIDKVT KADVRRIANQ
IFTETNRSIA TIQTAAPQKG AQQ
//
