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Database: UniProt
Entry: B9KZN6_THERP
LinkDB: B9KZN6_THERP
Original site: B9KZN6_THERP 
ID   B9KZN6_THERP            Unreviewed;       421 AA.
AC   B9KZN6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Processing protease {ECO:0000313|EMBL:ACM05545.1};
GN   OrderedLocusNames=trd_1505 {ECO:0000313|EMBL:ACM05545.1};
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC   Thermomicrobiaceae; Thermomicrobium.
OX   NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05545.1, ECO:0000313|Proteomes:UP000000447};
RN   [1] {ECO:0000313|EMBL:ACM05545.1, ECO:0000313|Proteomes:UP000000447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2
RC   {ECO:0000313|Proteomes:UP000000447};
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP001275; ACM05545.1; -; Genomic_DNA.
DR   RefSeq; WP_015922453.1; NC_011959.1.
DR   AlphaFoldDB; B9KZN6; -.
DR   STRING; 309801.trd_1505; -.
DR   KEGG; tro:trd_1505; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_0; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000000447; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ACM05545.1};
KW   Protease {ECO:0000313|EMBL:ACM05545.1}.
FT   DOMAIN          13..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          168..341
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   421 AA;  47457 MW;  23940F8FF8F97F5C CRC64;
     MDYQKTCLPN GIRIVTSRMP HVRSATVIVY VGVGSRYESD RLAGISHFLE HMLFKGTERR
     PDPVLISEAI EGVGGMMNAS TGREHTDYWV KVPSRHLELA FDVLADMLRH SLFDPGELEK
     ERHVIVEEIH GIRDTPDDYV HDLVDRALWN GHPLGRPIIG SEETVEAITR DELIAYLEQH
     YRADRLVVAA AGDLTHEQVI ELVQRYFGDL EPGTPADPHP ARLSDARPTI ELLERPTEQA
     HLCLALPALP YRDERRFVQG MLDSVLSSGM SSRLFKEIRE RQGLAYEVYG YLREYADVGQ
     AVIYTGTDVE RAERALRAVR GELEKLVREP VPDDELERTK ELRVGRIVMG LEDSRAVASW
     IGGQELVFGE VLTPEEVIAR IRAVTSEEIQ ALAQELFQPE RFALAVIGPF ADVEPLVCAV
     R
//
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