ID A0A1I4LWU0_9RHOB Unreviewed; 606 AA.
AC A0A1I4LWU0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SFL95412.1};
GN ORFNames=SAMN04488042_102269 {ECO:0000313|EMBL:SFL95412.1};
OS Shimia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=254406 {ECO:0000313|EMBL:SFL95412.1, ECO:0000313|Proteomes:UP000199144};
RN [1] {ECO:0000313|EMBL:SFL95412.1, ECO:0000313|Proteomes:UP000199144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15283 {ECO:0000313|EMBL:SFL95412.1,
RC ECO:0000313|Proteomes:UP000199144};
RA de Groot N.N.;
RL Submitted (OCT-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; FOTQ01000002; SFL95412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4LWU0; -.
DR STRING; 254406.SAMN04488042_102269; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000199144; 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:UP000199144};
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 348..591
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 68624 MW; FB6EF35900BE5AE7 CRC64;
MLHLPFPVRD ANPTSGSEGL GNLPEWNLSD LYNGDDAPEL LADLEWLESE CAAFAADYEG
KLAELSAADL LTCVQRNEKI SQVSGRIMSY AGLRYYQLTT DAERAQFMAN CQEKLTNFST
PLVFFTLELN RLEDEKLSAA FAENAGLARY EPVFRRIRAM KPYQLSDELE RFLHDLGVVG
DAWERLFDET IAGLTFEVEG EEYNIEGTLN FLTDPNRDKR EAAAHELARV FSDNIKIFSR
VHNTAAKEKE VVDRWRNMPT AQTGRHLSND VEPEVVEALR DAVVAAYPKL SHRYYELKRK
WLGLDRMQVW DRNAPLPMED PRTISWDEAR KMVMDAYTAF DPRMGELAEP FFDKGWIDAA
VKPGKAPGAF AHPTVTNVHP YVMLNYLGKP RDVMTLAHEL GHGVHQVLAA EQGEMLSSTP
LTLAETASVF GEMLTFRKML ETAETTEQRK VMLAGKVEDM INTVVRQIAF YDFECKLHAA
RRESELTPDD INALWMSVQA ESLGEAFDFM EGYETFWAYI PHFVHSPFYV YAYAFGDGLV
NALYAVYAEG GEGFEDKYFD MLKAGGSKHH KELLAPFGLD ASDPKFWDKG LSMISDMIDE
LEAMEA
//
