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Database: UniProt
Entry: J2FY93_9SPHN
LinkDB: J2FY93_9SPHN
Original site: J2FY93_9SPHN 
ID   J2FY93_9SPHN            Unreviewed;       979 AA.
AC   J2FY93;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:EJL22225.1};
GN   ORFNames=PMI02_04775 {ECO:0000313|EMBL:EJL22225.1};
OS   Novosphingobium sp. AP12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL22225.1, ECO:0000313|Proteomes:UP000007515};
RN   [1] {ECO:0000313|EMBL:EJL22225.1, ECO:0000313|Proteomes:UP000007515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP12 {ECO:0000313|EMBL:EJL22225.1,
RC   ECO:0000313|Proteomes:UP000007515};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EJL22225.1}.
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DR   EMBL; AKKE01000156; EJL22225.1; -; Genomic_DNA.
DR   RefSeq; WP_007687136.1; NZ_AKKE01000156.1.
DR   AlphaFoldDB; J2FY93; -.
DR   STRING; 1144305.PMI02_04775; -.
DR   PATRIC; fig|1144305.3.peg.4398; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000007515; 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; 3.
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; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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:UP000007515};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..979
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003747273"
FT   DOMAIN          88..225
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          238..422
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          739..900
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   979 AA;  106049 MW;  69F7C9C4001C14B9 CRC64;
     MTTSPRAART LACLLLLQAP IPPLLAQEVA PQPAAAPASA PMATPIVGQS DPWLYRGSDI
     PHDPEWHFGE LPNGIKYAVR KNGVPPGQVS IRIRVDAGSL YETDAERGYA HLLEHMLFRQ
     SKYLPEGTAI AAFQRLGATF GSDTNAVTST TQTVFKLDLP NATPTSLDET FKLMSGMVTA
     PTLSASNLKS DLPIVLAEMR ERGGASKRVQ DAMQKVLYAG QPLANREPIG TLESLTSATP
     ESVRAFYSRW YRPDNVAVIV AGDVDPAMLE SYVKKWFTDW SAKGKKAPAP SFGDPVAPKG
     ADPKNPVGET RVLVEPDLPP SLMYAVLRPW RQVNDNIVYN QGLMTDAIAQ AIINRRLESK
     ARAGGSFLSA SVNQDDVSRS ADATFVSVTP LGDDWQGALR DVRSVIADAL TRAPTQVEID
     REAAELDVAF QVPVEQQRIL PGSKLADDLV NALDIRETVA APNDVLRIFR ESQPLFTPDA
     VLKHTRQLFT GTVTRGLFTV QEQGKATDRQ LQLALAEPVK ADASVRAALA PVSFEKLPAI
     GKAAKAVTDL PTGLLEIEQL TFANGVKALL WPVAEEPGRV MVKTRFGGGY RSVDPKDAAY
     ITLGNYALVG SGLATLGQDD LDRISTGRKM GFDFEVQDAA FELSAETRPQ DLADQLYLFA
     AKLDLPRWDV NPVMRAKAAA KVQYATFSTS PQGVLNRDLQ FYQRGEDARF ATPTPEEIEA
     TTADGFKRVW SKALKEGPVE VQIFGDFDKT AAIAALEKTF GALKARQPVA VSTAEVKIPV
     PQPSDKPVTL VHHGDPDQAA AVISWPTGGG VMGIRESRQL EILTQLFTNR LMDAVREKLG
     VSYAPYVYST WPVDLAAGGS ITAMAQLDPK SVPIFFQTAD EIAQNLINNP PTADELALVV
     EPLRQQVTRA ASSTSFFMSQ LEGATSDPSR IGTVRTVLSD YTVTTPQAMQ ALAARYLGKD
     HSWRLEVMPE GKDAKVAAK
//
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