ID J9QTP5_RIEAN Unreviewed; 954 AA.
AC J9QTP5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Zn-dependent peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B739_1685 {ECO:0000313|EMBL:AFR36276.1};
OS Riemerella anatipestifer RA-CH-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR36276.1, ECO:0000313|Proteomes:UP000006276};
RN [1] {ECO:0000313|EMBL:AFR36276.1, ECO:0000313|Proteomes:UP000006276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR36276.1,
RC ECO:0000313|Proteomes:UP000006276};
RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT "Riemerella anatipestifer vaccine strains.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP003787; AFR36276.1; -; Genomic_DNA.
DR RefSeq; WP_014938572.1; NC_018609.1.
DR AlphaFoldDB; J9QTP5; -.
DR STRING; 34085.AB406_1796; -.
DR KEGG; rag:B739_1685; -.
DR PATRIC; fig|1228997.3.peg.1684; -.
DR HOGENOM; CLU_306466_0_0_10; -.
DR Proteomes; UP000006276; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006276};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 37..85
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 241..412
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 727..848
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 95..127
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 954 AA; 109833 MW; D3B31C4775A80772 CRC64;
MKYDVISHTD KNGLEYLSVT NDDNQVRIYT LKNGLKVYLS KNSDAPRIQT YIPVRTGSNN
DPKDNTGLAH YLEHMMFKGT SKIGSLDWEK ERPLLQKLSD LFEQHKATQN EEEKKQIYKE
IDSISQEAAQ YAIPNEYDKI LSSLGASGTN AHTWLDETVY KNNIPSNELE KWFKVEKERF
SELALRLFHT ELESVYEEFN RAQDNDFRLV HYEIMDALFP NHPNGQQTTL GKAEHLKNPS
MEALHKYFNE YYVPNNYALI LVGDLDFEPT IALAERYFGT FSFRELPPKT PIIEQPISNI
IKRTIKSPSA PRLQVAWRSH SYGTQEARLT EICTQILSNN GEVGLIDLNI NQKQTALRAS
AFHSPFKSYG FLSIVIVPKE NQTLDEAKDL ILSQIEALKK GDFPDWLIPA IINDIKKGRL
KQLETADGLA TLLYETFIKE REWNEELNEL NLYETITKKE VISFANEFFG ENYVVVYKER
GENDKLIRVE NPKITPIKIN KEAQSEFLTQ LLAEKTHDIA PIFADYSKEI LEDSLNGIKL
SSIKNTQNNL AQMNFIFPMG TDNDKELGLV LEVLEYMGTD RYSPEEIKQE FYKIGVNYSF
QVGTDNISIM LGGLEENLAK GVALMVHWLR NIQPDNSIYQ TMVATILDAR EISKKDKNQI
TRALVNYAKY GENSRFRDVI TKERLQTAKA EDFTQRTQIL LDYPYELFFY GQDIEAFKSA
LLDIGLTKGN LTPPAPKNYP EPLTNQNKVY LVDYDMVQVE IMKVGRGEEI NPKYFGRISV
FNEYFGRGLS SIVFQEIRES KSLAYSAYVS YTYPSQLKKY DYVTSYLGTQ ADKMEIALNS
INELMSELPQ IKSQFSNAKS SALKQIASQR LTKQNLYFNY LAMQKWGYSY DIRKDIYDEV
NSLSLDDLTD FYNQNIKPIP YHTAIIGQTK SLDLNYLKSL GTVQELSIED LFGY
//
