ID A0A0S8D7S6_9BACT Unreviewed; 589 AA.
AC A0A0S8D7S6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK69_00570 {ECO:0000313|EMBL:KPK31389.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK31389.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK31389.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK31389.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK31389.1}.
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DR EMBL; LJNR01000004; KPK31389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8D7S6; -.
DR Proteomes; UP000051394; Unassembled WGS sequence.
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; cd09610; 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; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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 111..177
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 198..577
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 589 AA; 67614 MW; 972363692D1689D7 CRC64;
MAKGIVWNLE DLYQGQEDPR LDQDLEAARE KAQAFSSLYK GKIRDEDLEA QTLLSAIQAY
ESIHELGMKP YAFAYLSHAS DVRDPKRNAL FQRVQEAWND ILEMITFFPL EIMALPESSL
RRLGENDALQ SYRHFLLQQT KLKPHALSEP EETIMQLMRL SGRKAFVSFY DEFMASIQVA
LEIDGQVKSF SVEQLLSLLH GPDRSVRENA YQALLEELDR QSVVLRNIIN ALLLDHRLET
LKRRYPSPMH RACITDGVDE GIIGGMMEVV EAHYPLARRY FCEKAALLGL NRLDTTDLWA
PLNAEGTPIP FSKARGFVLE AMETFHPSFY SIAHEFFERN WIHAESRKGK RSGAFCRCFA
PSQHPFVLMN YSGNLRDVAI LAHELGHGIH YQLASRQSFL GFDPSPVLAE TASTFSEILL
IQHLLKSKAL QAQTPPLLSS HLDGIMVTVY RQNVLTRFEQ AIHRERQNQL LSTEEICQLW
WEENERLYRE EVEMIPAYRW GWAHVPHFIH HPFYCYSYIF GNLLAIALYQ HFQNNGEDFS
EKIISLLSAG ASQAPIDLLA QLGLDPAQKS LWEQAFRYVE KLIDALEGV
//
