ID W0RDG2_9BACT Unreviewed; 473 AA.
AC W0RDG2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:AHG88350.1};
GN ORFNames=J421_0813 {ECO:0000313|EMBL:AHG88350.1};
OS Gemmatirosa kalamazoonensis.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG88350.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG88350.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG88350.1,
RC ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP007128; AHG88350.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RDG2; -.
DR STRING; 861299.J421_0813; -.
DR KEGG; gba:J421_0813; -.
DR PATRIC; fig|861299.3.peg.827; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_1_0; -.
DR InParanoid; W0RDG2; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000019151; 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:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 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:UP000019151};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..473
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004795391"
FT DOMAIN 44..178
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..378
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 473 AA; 51490 MW; 8BBF55BC71AFE1C1 CRC64;
MRLTSLLRPT ALALAVAVAP PLSAQATAIS IPNERMTLPN GLQVLLAPDH STPRVTVDVW
YHVGSKNEVP GRTGFAHMFE HVMFTGSGHV PYGLHDRLTE GVGGDNNGST TEDRTNYYEN
VPSNYLESAL WMEADRMGFL LDKLDEAKFS AQRDIVQNER RQRTDNQPYG RAFEIVTAAM
VPAANPYSWP VVGYMSDLKQ ATVEDVKNFF RLYYAPSNAT LAIVGDFDPA QAKAWVRKYF
SDLPRGAAIT RPSVPAVTMP NEKRLVYEDR VQVPRLYVAW PSVGETGPDR HALDLLGEVL
TSSRTARLTK ALVYDRQSAA SVNAGQNTNE NAGAFFVLAT PRPGHTLAEL EATTDSVLER
LKREGPTAEE IAKAKAGLEF GFVNGLQSNL GKAEILNSGA VFHGDPGYFQ QEYAALKAVT
AADVQRVANK YLGAGRVVLS VVPQGKRELA AKAEASTPVA VSPDGGHYIM ESK
//
