ID A0A0S8HQG0_9DELT Unreviewed; 611 AA.
AC A0A0S8HQG0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ94_16925 {ECO:0000313|EMBL:KPK87486.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK87486.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK87486.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK87486.1};
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:KPK87486.1}.
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DR EMBL; LJUR01000199; KPK87486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HQG0; -.
DR STRING; 1703399.AMJ94_16925; -.
DR PATRIC; fig|1703399.3.peg.2991; -.
DR Proteomes; UP000051218; 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 122..189
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..587
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 611 AA; 70831 MW; 5D070E7B3B76F5CD CRC64;
MERQKNMAPN PEDRSITWDL TDLYPAPREP AWEEDLKQGL DRARQFQGFY KNADLTALSP
AAFLQALKDY ESIQEEGVKP FLYASLLFSE DSQNVEYKTL LQKAKEQWNE LENQLLFFRL
ALIDLPEEKL RELLVHPPLK VYEHALRFLR RFRPFTRGEK EEEILNRKNL TGRSAFTTLF
DEFTGSFSFR IEVEGEEKEL TGSQVLSLLY SPDRSLRERA FRTFLERHGE NHLVLGSIFN
ALILDAQVED DLRGYQGPMH RTHLENEISA ETVELMMEVT ESHYALAQEY FQAKACLLGL
PKLKNYDLYA PLPGGRKEIP FDEARGLLLQ SFRDFHPLFG RIAGEFFEKR WIDAPPRKGK
YGGAFCTGMT PSLHPYILLN YTGHLRDVLT LAHEMGHGIH FYLARKQNLM NFDPPLTLAE
TASVFGELVM TQALLREERD LAVRLALLCI EIEDMIATVF RQNVLTRFEQ QVYQRRRERL
LSSEEAGDLW LQANARLFGD SVEMIPEYRW GWAYISHFIH SRFYCYSYIF GELVSLALFQ
KYEEEGSSFL DPLIHLLERG GSASPQELLK EAGVDIARAD FWQKGFRVIR QLLDELKSLG
PWDKICVGPP A
//