ID A0A2Z5G5B9_9BACT Unreviewed; 741 AA.
AC A0A2Z5G5B9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dipeptidyl peptidase IV {ECO:0000313|EMBL:AXC14281.1};
GN ORFNames=ACPOL_5021 {ECO:0000313|EMBL:AXC14281.1};
OS Acidisarcina polymorpha.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC14281.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC14281.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC14281.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
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DR EMBL; CP030840; AXC14281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5G5B9; -.
DR KEGG; abas:ACPOL_5021; -.
DR Proteomes; UP000253606; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000253606};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..741
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016381832"
FT DOMAIN 118..454
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 538..734
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 741 AA; 82956 MW; CBAA7CF15D25BF56 CRC64;
MKVLIGLLLS LLAPLQNPFA AEVQRPITVE DIYAHGNPTG WMPEELQWSP DGARVTFLSS
DSDLMELNPN NGSIGTLVSH TKLGSLASKA ANEKDRDHRS RYGMSSYIWA PDSKHILFDS
DGQLFLYSLD NGTAIDVAST GVGSGDDPKF SPNGQYLSYV RDHNLFVHRF KDQSAEVALT
NTHDEALLNG EVDWVYLEEL DVRTNYVWAP DSARVAYLQM NEESVPEYPI TDWVPIHATV
DRQRYPQPGD PNPQVRLGVV KAQGGKTLWM KLPISEGNDY IPRFGWVNPE TLWIEILTRD
QKHRSIYFAD AQHGDVRLAY SEQDEKFLDN YDVEFSRGNF YLLSWRDGHT HIYDYAFDQA
NPLSGAVAEP SAHLVRQITS GDFEVTHLEP VVENSQTIFF ISNESDPREM QVWAIQTDGT
GKRRLSTSAG VHSPVFAPSS STFIDTASDR TTPPRVDLCH GSDCRPFWKS QPLEGVTITA
PVSLQLTAAD SKTTLYAELL LPSGEKPASL PLIMNPYGGP HAQTVQNSWR STQDRMWDQL
LLQHGFAVLR VDNRGMGARG RDFEQAAYHN FGPVQLADQL AALDQVLAKY PQLDKDRLGW
WGWSWGGTFT LNAMTHSDRF RAGVPVAPVT DWRNYDSIYT ERYMGLPAEN ADGYRDQSVV
NSASHLKGHL LIAHGTGDDN VHLANTMQFI QALIDADLPY DYQVYPRKTH SIAGAEARTQ
LFNRILAHFE TYLKPVAGSA P
//
