ID A0A1M6J409_9RHOB Unreviewed; 606 AA.
AC A0A1M6J409;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SHJ41397.1};
GN ORFNames=SAMN05444000_10899 {ECO:0000313|EMBL:SHJ41397.1};
OS Shimia gijangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHJ41397.1, ECO:0000313|Proteomes:UP000183982};
RN [1] {ECO:0000313|Proteomes:UP000183982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; FQZQ01000008; SHJ41397.1; -; Genomic_DNA.
DR RefSeq; WP_073251750.1; NZ_FQZQ01000008.1.
DR AlphaFoldDB; A0A1M6J409; -.
DR STRING; 1470563.SAMN05444000_10899; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000183982; 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 Reference proteome {ECO:0000313|Proteomes:UP000183982};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 128..196
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 351..591
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 606 AA; 68668 MW; 4E6A304FE5F1B704 CRC64;
MRDLPFPVFD ANSSHGTEGL GNLPEWDLSD LYTGEDAPEL EADMAFLEKE CAAFAADYQG
KLGDLDAKGL LECVQRNEKI SSVSGRIMSY AGLRYYQMTT DAERAQFMSN CQEKLTDFTT
PLVFFTLELN RLEDNALETA FAQNAELARY KPVFDRIRAM KPHQLSDELE KFLHDLGVVG
DAWERLFDET IAGLTFDIEG QELNIEATLN YLTEQDRAKR EMASRELARV FAENIKIFAR
VHNTSAKEKE VVDRWRNMPT AQTGRHLSND VEPEVVEALR DAVVAAYPKL SHRYYELKRK
WLGLDRMQVW DRNAPLPMED TKTVGWEDAR KMVMDAYTAF DPRMGDLAAP FFDKGWIDAE
VKPGKAPGAF AHPTVTDVHP YVMLNYLGKP RDVMTLAHEL GHGVHQVLAA DQGEMLSSTP
LTLAETASVF GEMLTFRKML DNAETQEQRK ILLAGKVEDM INTVVRQIAF YDFECKLHAA
RRESELTPDD INALWMSVQA ESLGEAFDFM DGYETFWAYI PHFVHSPFYV YAYAFGDGLV
NALYAVYAEG DAGFEDKYFD MLKAGGSKHH KELLAPFGLD ASDPKFWDKG LSMISSMIDE
LEAMED
//
