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Database: UniProt
Entry: G5KHH6_9STRE
LinkDB: G5KHH6_9STRE
Original site: G5KHH6_9STRE 
ID   G5KHH6_9STRE            Unreviewed;       597 AA.
AC   G5KHH6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EHJ55770.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:EHJ55770.1};
GN   Name=pepF_2 {ECO:0000313|EMBL:EHJ55770.1};
GN   ORFNames=STRUR_1491 {ECO:0000313|EMBL:EHJ55770.1};
OS   Streptococcus urinalis 2285-97.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ55770.1, ECO:0000313|Proteomes:UP000005388};
RN   [1] {ECO:0000313|EMBL:EHJ55770.1, ECO:0000313|Proteomes:UP000005388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2285-97 {ECO:0000313|EMBL:EHJ55770.1};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ55770.1}.
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DR   EMBL; AEUZ02000001; EHJ55770.1; -; Genomic_DNA.
DR   RefSeq; WP_006738559.1; NZ_AEUZ02000001.1.
DR   AlphaFoldDB; G5KHH6; -.
DR   STRING; 764291.STRUR_1491; -.
DR   eggNOG; COG1164; Bacteria.
DR   Proteomes; UP000005388; Unassembled WGS sequence.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHJ55770.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005388};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          199..579
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   597 AA;  69042 MW;  3CC7E69C09E704F1 CRC64;
     MKLKKRSEFP ETELWDLTAL YKDRNDFLLA IEKALEDVNS FKRNYKNHLN TKKDFEMALF
     EIEQIYIQIS HIETYSFMPQ TTDFSSDEFA QIAKAGDDFV TKASVELSFF DTALANADTD
     ILDALEKNDY FKAIIRQAKI QKAHLLTPEV EETITNFREI LNAPYDIYTK MRAGDFEMEN
     FTVNGKQYEN SFVSYENFYQ NHEDADVREK AFRSFSKGLR KHQNTAAAAY LSKVKSEKLI
     ADMKGYASVF DYLLAEQEVD KSMFDRQIDL IMTKFGPVAQ KFVKHVAQVN GLEKMTFADW
     KLDIDNELNP EVTIDDAYKL VMDSLKPLGQ EYLTEIERYQ TERWVDFAAN ENKDSGGYAA
     DPYKVHPYVL MSWTGRMSDV YTLIHEIGHS GQFIFSDNAQ SYFNTHMSTY YVEAPSTFNE
     LMLSDYLENQ FDQPRQKRFA LAHRLTDTYF HNFITHLLEA AFQRKVYNLI EDGGTFGAEQ
     LNHIMKDVLT EFWGDAIEID DDAALTWMRQ SHYYMGLYSY TYSAGLVIST TGYLHLKSHP
     NGAKDWLAFL KSGGSRTPIE TAKLIGADIS TDKPILDTID FLDKTVEQII TYTNEIN
//
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