ID G4FM27_9SYNE Unreviewed; 705 AA.
AC G4FM27;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=Syn8016DRAFT_1079 {ECO:0000313|EMBL:EHA64037.1};
OS Synechococcus sp. WH 8016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA64037.1, ECO:0000313|Proteomes:UP000002752};
RN [1] {ECO:0000313|EMBL:EHA64037.1, ECO:0000313|Proteomes:UP000002752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT "The draft genome of Synechococcus sp. WH 8016.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC Ala commonly occur as P1 or P1' residues, but more distant residues
CC are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC Evidence={ECO:0000256|ARBA:ARBA00024603};
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|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA64037.1}.
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DR EMBL; AGIK01000001; EHA64037.1; -; Genomic_DNA.
DR RefSeq; WP_006853220.1; NZ_AGIK01000001.1.
DR AlphaFoldDB; G4FM27; -.
DR STRING; 166318.Syn8016DRAFT_1079; -.
DR MEROPS; M03.A01; -.
DR PATRIC; fig|166318.3.peg.1162; -.
DR eggNOG; COG0339; Bacteria.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000002752; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF83; LD37516P; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF19310; TOP_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 29..155
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 241..699
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 705 AA; 79233 MW; 1C075CE6D6ED9950 CRC64;
MTKPELLRGH GLPRFEAIDA SQVKAHIPAL IQELEDQLSM LESTLQQRLS DNTPLSWDEV
MTPLHLLGER LRWSWGVVSH LNGVCNSPEL REAHAAQQPD VVRFSNRAGQ SQVIHQALER
LQQNPSHPLD STQTRILDAE LLSMRHRGVG LNGAAQKSFN EASEQLASLS TRFSNHVLDA
TQGWTLLVHD ADQLKGIPER ALQALAAAAK AAGDQHRDGQ EPTALEGPWR LGLDMPRYLP
VLTHADNRHL RETVYRAQVS RASSGELDNT PLIEEILDLR SHQAARLGYQ NWAEKSLASK
MADNVEAVER LLEELRVAAL PVAEREIEEL RDCARRHGAT EADAFSAWDV SYWAEKLRQE
RFNLNQEALR PWFPLPQVLD GLFHLCERLF SIQIEAADGE APIWHQDVRF FRVSDQEGKP
LAAFYLDPFS RPASKRGGAW MDECLNRSRN SEGEITHPVA YLICNQTPPA GDIPSLMSFE
EVETLFHEFG HGLQHMLTTV EHPQAAGINN VEWDAVELPS QFMENWCLDR QTLMGMARHW
KTGEPLPEED YNKLRNSRTF MQGCGTLRQV HFALTDLRLH SVWSPELGQS PDAFRRSIAE
TTTVLPPIPE DRFLCAFGHI FAGGYSAGYY SYKWAEVLSA DAFAAFEEVG LDQEEDIQAT
GQRFRNTVLS LGGSQRPADV YKSFRGRTAS TEALIRHSGL AVAGR
//
