ID F8JDC2_HYPSM Unreviewed; 615 AA.
AC F8JDC2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative oligoendopeptidase F {ECO:0000313|EMBL:CCB64002.1};
GN OrderedLocusNames=HYPMC_0769 {ECO:0000313|EMBL:CCB64002.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB64002.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; FQ859181; CCB64002.1; -; Genomic_DNA.
DR AlphaFoldDB; F8JDC2; -.
DR STRING; 717785.HYPMC_0769; -.
DR KEGG; hmc:HYPMC_0769; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_5; -.
DR Proteomes; UP000000494; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000000494};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 136..204
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 222..601
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 615 AA; 69400 MW; 50B66D700DC968FA CRC64;
MRRWPLSDIT LAPQSATKLA DDRDALGNMP QWDLSDLYSG PGDPAIQRDL KEAAAEATRI
KATYQGRLAE LAKDGDKLIH PVKDYEKLSD LAGKLGSFSG LYYVLNQTDP ARAKFNADVS
EALTKLYTDL IFFELELNQI DDAVLESALK HESLKRYKPW FDDLRKEKPH QLDERIETLF
TEKSQTSRGA WNRLFDETMS ALRFEVEGEK EALSLEPTLN LLSHADEKKR EAGSKALSKV
FQANLPLFSR ITNTLAKDKE ISDRWHNFKD VSDSRNLANR VEGPVVDALV SSVRAAYPLL
SHRYYAMKAK WLGKKTLASW DRNAPLPDKP ERTITWSEAE QIVLRAYNGF APEMATIAKQ
FFDKNWIDAP VKPGKAPGAF SASTVPSVHP YVMMNYLGKP RDVMTLAHEL GHGVHQWLAR
DQGPLLAPTP LTLAETASVF GEMLTFRALI AETKDAREKK AMLAAKVEDM INTVVRQIAF
YTFERKVHEA RREGELTAEQ INGFWMDVQA ESLGPAIDLK PGYEVFWTYI PHFIHSPFYV
YAYAFGDCLV NSLYGLYAEA HPGFVAKYFD LLKAGGSKHH SELLAPFGLD ARDPQFWNKG
LKVIEGMIDE LETMS
//
