ID E8PQ28_THESS Unreviewed; 562 AA.
AC E8PQ28;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ADW22947.1};
GN OrderedLocusNames=TSC_c23450 {ECO:0000313|EMBL:ADW22947.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW22947.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW22947.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP001962; ADW22947.1; -; Genomic_DNA.
DR RefSeq; WP_015718207.1; NC_014974.1.
DR AlphaFoldDB; E8PQ28; -.
DR STRING; 743525.TSC_c23450; -.
DR KEGG; tsc:TSC_c23450; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_1_0; -.
DR Proteomes; UP000008087; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 104..158
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 179..547
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 562 AA; 64059 MW; E823FBEE9D2923BB CRC64;
METTWDLTPL FPGLESPEFQ AAWEGVRKRI GQLKEQVDQQ APLKEVLASL DALLEESTPL
WAYLYARFTA DTTDEAALAK LSELEVLFLD FARLRPRLTR YLALQDPEEA GPYRILVEEA
REEALHMMPE GEEVLAAELS LSGRQAWSKL HENLTSQITA VVDGEELPIT QVRNLYFRPE
EEVRKKAYQA ELKAWEGHEV PLAYALNGVK GEASVLNRRR GYRDDLEPSL HRNRITRKAL
MALLEAVRES LPLFHRYYLL KAKALGKERL DWWDLFAPIG KGRRWSLEEA RDFIREKLAT
LVPNAAKVAE TAFQERWMDL LPRKGKIGGA YCMGRGGGKS LILANYEESF ESVSTLAHEL
GHAYHNFALA RVPASLREVP MTLAETASIM NETLVVEAAL KEVSPEEGLL ILDAYLQGAA
QVVVDIYSRF LFESWVFEGR KARELSPREF KELMLKAQKE AYGEVLATHH AYMWAVKGHY
YGSDFYNYPY TFGLLFGLAV YQEAKEDPGF AGRYEELLAT SGMYRAKELA ARYGFDLESP
AFWRRGFAVL AEKVEELERR LA
//