ID A0A085FZR1_9ENTR Unreviewed; 494 AA.
AC A0A085FZR1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative peptidase {ECO:0000313|EMBL:KFC76956.1};
GN Name=yhjJ {ECO:0000313|EMBL:KFC76956.1};
GN ORFNames=GBAG_4072 {ECO:0000313|EMBL:KFC76956.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC76956.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC76956.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC76956.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KFC76956.1}.
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DR EMBL; JMPI01000071; KFC76956.1; -; Genomic_DNA.
DR RefSeq; WP_034499642.1; NZ_JMPI01000071.1.
DR AlphaFoldDB; A0A085FZR1; -.
DR STRING; 1006004.GBAG_4072; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000028653; Unassembled WGS sequence.
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; 1.
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:UP000028653};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..494
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001790715"
FT DOMAIN 50..157
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..376
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 494 AA; 55513 MW; 745190B9E918D523 CRC64;
MQGTKIRLLA GGLLLVAAAS NVQAEALQPD PAWQQGTLAN GFQWQVLATP QRPSDRIEIR
LMVNTGSLTE TNQQSGYSHF LPRLALTQSG SLQPLQARSL WQQSVDPKRP LPPVIVSYDY
TLFNLSLPNN RNDLLKEALT YLSDSSGKMA ITPETVNVGL QTQDMVATWP MDTKDNWWRY
RLQGSTLLGH DPAEDLKQPV DSEQLKAFYQ KWYTPDAMTL IVVGNVDSRS VADQINKTFG
TLTGKRETPA PVATLSPLKR TPVSLMTDSV RQDRLSLTWD NAWTPIRESS ALLRYWRADL
AREALFWHVQ QNLSKQNIQD LNLSFDCRVL YQRAQCGINL ESPNTKLDAN LATVGKELVS
VRDKGLSQEE FDALITRKKA ELAGLFATYA RTDTDVLIGQ RLRSLQNQVV DIAPEQYQKL
RQDFLNSLTL SGLNQDLRQQ LSQEMALVLL QPKGEPEYNM KDLQATWDKV MVPSKALPLT
DEPKQDVSDI PPAQ
//
