ID F7RXJ6_9GAMM Unreviewed; 679 AA.
AC F7RXJ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-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=A28LD_0975 {ECO:0000313|EMBL:EGN75362.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN75362.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN75362.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN75362.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(2011).
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:EGN75362.1}.
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DR EMBL; AFPO01000012; EGN75362.1; -; Genomic_DNA.
DR RefSeq; WP_007419952.1; NZ_AFPO01000012.1.
DR AlphaFoldDB; F7RXJ6; -.
DR MEROPS; M03.004; -.
DR PATRIC; fig|1036674.4.peg.963; -.
DR eggNOG; COG0339; Bacteria.
DR Proteomes; UP000053031; 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; 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; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000053031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 34..152
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 225..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 76281 MW; 54182A2DA37AB227 CRC64;
MTMNATNPLL GEFTHPPFSK IKAEHVQPAI EAGIAESRQA IEQVVGQTAP TWETLVAPLE
HVDDKLTKIW GPVSHLNSVM SEEALREAHD GCLELLSEYA TWVGQHEGLY QAYQALAAGP
EFTQLSEPQQ RVVTETIRDF KLSGVGLEDE AKKRYGEIQN RLSQITSQFS NQVLDATNHW
FAHVTDENEL TGLPESAIAG AKEAAEEKQL EGWVFTMDIP SYLPVMMYAD SGKLRETMYE
AYVTRSSELG PDAGKFDNTA IMQEILALRH ELAELLGFED FAEMSLATKM ADNTEQVVHF
LQDLARRSLP QAKEEMAEIK AFANKEYGVN ELNSWDIPYY AEKLKQNSYN ISDEQLRPYF
PEQKVVQGLF TVAERLFGIQ IKEAKAETWH PQVKYFEISD NSGELRAGFY LDLYARAKKR
GGAWMADCAV RRRLPDGQLQ LPLAYLTCNF NKPVGDKPAL FTHDEVITLF HEFGHGLHHM
LTKIDVAGVS GINGVAWDAV ELPSQFLENW CWEPEALAFI SGHYETGEPL PEDLLERMLA
ARNFQAAMQM VRQLEFSLFD MQIHQAGADV NIQGTLDAVR NQVSVVKPPA YNRFQHSFGH
IFAGGYAAGY YSYKWAEVLS ADAFARFEEE GIFNADTGRA FLENILEMGG SRDAMDLFKA
FRGREPDIAP LLRHSGIAA
//
