ID A0A0W1A5N5_9GAMM Unreviewed; 671 AA.
AC A0A0W1A5N5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=Lwal_2373 {ECO:0000313|EMBL:KTD76651.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD76651.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD76651.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD76651.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD76651.1}.
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DR EMBL; LNZB01000051; KTD76651.1; -; Genomic_DNA.
DR RefSeq; WP_058480992.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1A5N5; -.
DR STRING; 66969.Lwal_2373; -.
DR PATRIC; fig|66969.6.peg.2577; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000054729; 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; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 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:UP000054729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 26..140
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 215..669
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 671 AA; 76474 MW; 120032F9E853CA4D CRC64;
MSTTIGLPQF SRVDVNHFKT NLEALLKNNL ERIDHLLKEN HYYTWDNLMY PLDDLGDSLE
QMWSPFSHLH SVMDSKELRD CYEACLPLLS AYDAAIGHNH KLYQAIKSID QHSLDVAQKK
LIQDSLRDFE LSGVALSAKD KKRFEAIQAR LAELSSKFEN NVLDATQAFT VHLPDDTRIK
GLPEHAISTA KELAKEKDLP GYVLTLEYPS FQAVITHAED RSLREELYQA FVTRASEKGP
NAGEFDNSKI IDEILALRHE KAQLLGFKHY AELSLATKMA DTPNQVVDFM MDLVGRTRKK
GQIEFVELQQ FALEKYKFDS VNPWDVAYLS EKRRQDLFSL SQEELRPYFP QPKVMQGLFA
IVKKLYGMSI QEIPGVDVWH KDVQCYCIVD EHNQVRGYIY TDLFARPNKR GGAWMDSMQS
RRKLEDGTIQ VPIATLTCNF AKASGNKPAQ LSHDEVVTLF HEFGHCLHHV LTQVDYLDGS
GINGVEWDAV ELPSQFFENW CWDKSSLVLL SSHVDTGAPL TDELYERLIA AKNFQSAMAM
LRQMEFALFD FRIHQEYNGI KESFVAETLA DVRTKTSVIP LAPYNRFQHS FSHIFGGGYA
AGYYSYMWAE VLSSDAFSRF EEEGIFNPKT GHDFLKAILE AGGSKKASDA FIEFRGRPAT
IDALLRHNGI I
//
