ID D4GGK1_PANAM Unreviewed; 502 AA.
AC D4GGK1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=YhjJ {ECO:0000313|EMBL:ADD75302.1};
GN Name=yhjJ {ECO:0000313|EMBL:ADD75302.1};
GN OrderedLocusNames=PANA_0135 {ECO:0000313|EMBL:ADD75302.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD75302.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD75302.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD75302.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP001875; ADD75302.1; -; Genomic_DNA.
DR RefSeq; WP_013024042.1; NC_013956.2.
DR AlphaFoldDB; D4GGK1; -.
DR STRING; 706191.PANA_0135; -.
DR GeneID; 57270222; -.
DR KEGG; pam:PANA_0135; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_043932_0_0_6; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
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; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..502
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003057270"
FT DOMAIN 51..158
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..377
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 476..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56152 MW; D5A1ADB198B534EC CRC64;
MQGTRIRLLV GGLVLAATSY GAPAETLQPD PAWQQGRLDN GFNWQLLATP QRPSDRIELR
MVVNTGSLVE SAQQTGFSHL LSRLALVHNT ALDTNQQRAL WQQSIDPQRP LPPVISSYDY
TQYNLSLPNN RPELLKEALN WLAATAGDMA ITNQVVDTAL SASDPVRTWP ADTQDVWWRY
RLKGSALLAH DPAEKPRAPV DVAQLKSFYQ QWYTPDAMTL YVVGNVDSRN LSEQINKAFS
PLEGKRSAPA SMPTLSPLPH DPVNLVSGTL AQDRLSLVWD TPWQPIRDSQ NLQRYWRSDL
AREALFWHVQ RAMSNKKVQG VQVGFDCRVL YQRAQCSINM DTRNDSLEQN MNLVARELAA
VRDNGLPQEE FDALMAQKLL ELNKLFTTYA RTDTDVLISQ RLRSQRNSVV DIAPEQYQKL
RQDFLSGLTR DQLNQELRQQ LSQELMMVLI QPEGESETNV KSLKTGWDKL MTLPATASAP
AAGGDVSQPD SNAAGDAAPP TS
//
