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Database: UniProt
Entry: A0A160JG98_9PROT
LinkDB: A0A160JG98_9PROT
Original site: A0A160JG98_9PROT 
ID   A0A160JG98_9PROT        Unreviewed;       604 AA.
AC   A0A160JG98;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ANC91975.1};
GN   ORFNames=A6A40_08665 {ECO:0000313|EMBL:ANC91975.1};
OS   Azospirillum humicireducens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91975.1, ECO:0000313|Proteomes:UP000077405};
RN   [1] {ECO:0000313|EMBL:ANC91975.1, ECO:0000313|Proteomes:UP000077405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91975.1,
RC   ECO:0000313|Proteomes:UP000077405};
RX   PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA   Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT   "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT   from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
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; CP015285; ANC91975.1; -; Genomic_DNA.
DR   RefSeq; WP_063635053.1; NZ_CP015285.1.
DR   AlphaFoldDB; A0A160JG98; -.
DR   STRING; 1226968.A6A40_08665; -.
DR   KEGG; ahu:A6A40_08665; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000077405; 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   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;  68076 MW;  9DCD3975E28C26D9 CRC64;
     MTSSAAMAAN DTPELGALPT WDLSDLYPGM DSPELKADLD RMERECKAFR ERYAGKLAAL
     KGDDLAAAIR SYEEIDETLS RVMSYAGLVY NGNMVDPTIA KFYQSAQERV NDISAHLIFF
     TLEINRLDEA DLAAKQTASL ALRHYEPWLR DVRLYRDHQL SDEIERLLHE KHVVGRAAWN
     RLFDETIASL RFPMGGKDLT CAEALNRLSD RNPAIRREAG EVVGKVLGEN ARLFALVTNT
     LAKDKEIEDD WRNYPTPTSA RNLSNRVEDE VVDALVSAVK GAYPDLSHRY YAMKAKWFGQ
     DHLDYWDRNA PLPEDADRSI PWEEARDIVL GAYGRFSPDL ASLGKRFFDN PWIDAPVRPG
     KAPGAFAHPT VPSVHPYLLV NYQGKTRDVM TLAHELGHGV HQILAGKQGH FLSDTPLTLA
     ETASVFGEML TFRALLAAET DPKRRRIMLA GKVEDMLNTV VRQIAFFDFE RRVHTERREG
     ELTSDRIGEI WMAVQTESLG PALRFDEGYR HYWSYIPHFI HSPFYVYAYA FGDCLVNSLY
     AVYQDAEKGF AEKYLAMLSA GGTLRHKELL APFGLDASDP AFWQKGLGVI RGFIDELEAG
     EATG
//
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