ID A0A1X7H7G3_9PROT Unreviewed; 604 AA.
AC A0A1X7H7G3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SMF81111.1};
GN ORFNames=SAMN02982917_5154 {ECO:0000313|EMBL:SMF81111.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF81111.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF81111.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF81111.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXAK01000007; SMF81111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7H7G3; -.
DR STRING; 286727.SAMN02982917_5154; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000192936; 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 123..192
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 209..588
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 604 AA; 68252 MW; 9BDCE529968C531B CRC64;
MTSSAATAAN DTPDLGALPT WDLSDLYPGT ESPELKADLD RMERECKAFR ERYAGKLAAL
NGDDLAAAIR KYEDIDETLS RVMSYAGLVY NGNMVDPAIA KFYQSAQERV NDISAHLIFF
TLEINRLDDK DLAAKQKASS ALRHYEPWLR DVRLYRDHQL SDEIERLLHE KHVVGRAAWN
RLFDETIASL RFPMGGKELT CAEALNRLSD RNPAVRREAG ESVGKVLGEN ARLFALITNT
LAKDKEIEDD WRNYPTPTSS RNLSNRVEDE VVDALVSAVK SAYPELSHRY YAMKAKWFGQ
DHLDYWDRNA PLPEDADRSI PWDEARDIVL GAYGRFSPDL ASLGKRFFDN PWIDAPVRPG
KAPGAFAHPT VPSVHPYLLV NYQGKTRDVM TLAHELGHGV HQILAGRQGH FLSDTPLTLA
ETASVFGEML TFRALLAAET DPKRRRIMLA GKVEDMLNTV VRQIAFFDFE RRVHTERREG
ELTPERIGEI WMAVQVESLG PALRFDEGYR HYWSYIPHFI HSPFYVYAYA FGDCLVNSLY
AVYQDAEKGF AEKYLAMLEA GGTLRHKELL APFGLDASDP AFWQRGLGVI RGFIDELEAG
EAKA
//
