ID B9XFB9_PEDPL Unreviewed; 530 AA.
AC B9XFB9;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:EEF61617.1};
DE Flags: Precursor;
GN ORFNames=Cflav_PD4296 {ECO:0000313|EMBL:EEF61617.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF61617.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF61617.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF61617.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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:EEF61617.1}.
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DR EMBL; ABOX02000009; EEF61617.1; -; Genomic_DNA.
DR AlphaFoldDB; B9XFB9; -.
DR STRING; 320771.Cflav_PD4296; -.
DR Proteomes; UP000003688; 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; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000003688};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 65..99
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 274..450
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 104..134
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 530 AA; 60711 MW; 57190EA38B0578D9 CRC64;
MWLNWVMHNS MVDISKRLSK LTFTFFIAAT CAASAWAQKV PVTEVTLDNG MKLLMVERHD
EPSISGGWVA HVGASNERPG ITGIAHLFEH MMFKGTPTIG TKDYKKDQQI IAEQEEVRNE
MRKEEAKIRA AYRRGEIDDL TKPENQTPHW KGLNRKFNEL IAQQRDILVK NEFDQVYTKE
GGTGMNAFTS EDMTAYFITV PANKMQLWMW MESERIFHPV FREFYAERDV VFEERRMRTD
STPLGKFTEE SEAMFWESSP YHWPVVGWPS DIPSISKAQA DEFYGLFYAP QNLTLILVGD
FKTNDVVLLA KKYFERIPRG KKDPPDVVTQ EVPQAAEKRM YAEAETNPQV DINWHTVPFG
HKDSYPLEVL AQILSTRTGR LYKGLVLGSQ VATETYAAQD SRKWAGLFNA GGEARDGKTP
EEVEQGIYTE MEKLKKEEVP AEELQKVKNN FAASEYRRLT ANMPILMHLI QNEGEGDWRE
INEAGKKIQL VTAADVKRVA NKYFTKENRM VGIYTRKGSS SKQEGNNEGK
//
