ID B1I7P3_STRPI Unreviewed; 598 AA.
AC B1I7P3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ACA35537.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:ACA35537.1};
GN Name=pepF2 {ECO:0000313|EMBL:ACA35537.1};
GN OrderedLocusNames=SPH_1897 {ECO:0000313|EMBL:ACA35537.1};
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA35537.1, ECO:0000313|Proteomes:UP000002163};
RN [1] {ECO:0000313|Proteomes:UP000002163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP000936; ACA35537.1; -; Genomic_DNA.
DR RefSeq; WP_000435570.1; NC_010380.1.
DR AlphaFoldDB; B1I7P3; -.
DR SMR; B1I7P3; -.
DR GeneID; 66806857; -.
DR KEGG; spv:SPH_1897; -.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000002163; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09609; 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; IPR034009; M3B_PepF_4.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR004438; Peptidase_M3B.
DR NCBIfam; TIGR00181; pepF; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACA35537.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 199..578
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 17..44
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 598 AA; 68656 MW; 63C7441E0F6FD911 CRC64;
MEQKHRSEFP EKELWDLTAL YQDREDFLRA IEKAREDINQ FSRDYKGNLH TFEDFEKAFA
ELEQIYIQMS HIGNYGFMPQ TTDYSNDEFA NIAQAGMEFE TDASVALTFF DDALVAADEE
VLDRLGKLPH LTAAIRQAKI KKAHYLGADV EKALTNLGEV FYSPQDIYTK MRAGDFEMAD
FEAHGKTYKN SFVTYENFYQ NHEDAEVREK SFRSFSEGLR KHQNTAAAAY LAQVKSEKLL
ADMKGYDSVF DYLLAEQEVD RVMFDRQIDL IMKDFAPVAQ RYLKHVAKVN GLEKMTFADW
KLDLDSALNP EVTIDDAYDL VMKSVEPLGQ EYCQEVARYQ EERWVDFAAN SGKDSGGYAA
DPYRVHPYVL MSWTGRLSDV YTLIHEIGHS GQFIFSDNHQ SYFNAHMSTY YVEAPSTFNE
LLLSDYLENQ SNDPRQKRFA LAHRLTDTYF HNFITHLLEA AFQRKVYTLI EEGETFGASK
LNSIMKEVLT DFWGDAIEID DDATLTWMRQ AHYYMGLYSY TYSAGLVIST AGYLHLKHSE
TGAEDWLNLL KSGGSKTPLE SAMIIGADIS TDKPLRDTIQ FLSDTVDQII SYSAELGE
//
