ID A0A0Q6UG54_9CAUL Unreviewed; 955 AA.
AC A0A0Q6UG54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQV62007.1};
GN ORFNames=ASC62_00245 {ECO:0000313|EMBL:KQV62007.1};
OS Caulobacter sp. Root342.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736519 {ECO:0000313|EMBL:KQV62007.1, ECO:0000313|Proteomes:UP000051656};
RN [1] {ECO:0000313|EMBL:KQV62007.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV62007.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV62007.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV62007.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQV62007.1}.
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DR EMBL; LMDD01000001; KQV62007.1; -; Genomic_DNA.
DR RefSeq; WP_056053998.1; NZ_LMDD01000001.1.
DR AlphaFoldDB; A0A0Q6UG54; -.
DR STRING; 1736519.ASC62_00245; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051656; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..955
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006293129"
FT DOMAIN 63..178
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 218..397
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 534..637
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 679..855
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 955 AA; 100371 MW; 4E5533A86FD3FCA0 CRC64;
MIRTARLALV AAALSTTALS PLAMAATQAK AKPRTAAVAP VASAIKVPPI VYQQRVLANS
LKVFTSRDTT TPNVTVQVWY GVGSKDDPHG RSGFAHLFEH LMFKATRNMP SETLDRLTED
VGGFNNASTW DDFTNYYEVA PANHLERLIW AESDRLKSLV IDDAVFASER DVVKEELRQR
VLADPYGRFF ALSIPQQSFA THPYQRPGIG SIEELDAATV DDVRAFHATY YRPDNAALIV
VGNFDQAKLD AMIDQYFGPL TTPAGAIPKV TAVEPARTGP KTVTTYGPNV PLPALAITWL
APAAANKDTP ALAVLDAVLT AGKSSRLYDS LVYDQKIAQS VFSDAPNNAQ PGLFYVGAIM
AGGKTVQQGE TALRAQVARI RDGLVTPAEL AEAKTGLLAD AVRRREEIDG RGFAIGYALE
TEGDAASANT NLAKLQAVTA ADIQRVARKY LADDRRTVIR YLPEKDRPAG EKDVTPPIPK
VASVKFDGPV TTLAPEGERQ KPPAVAPPVP AVLPTPAEKT LANGLRVIVA KSSDLPLITA
DLTVRGGASS DPAGLAGASN LTAELLTEGT TTRSATQVAR ETEALGANLE AGSGWEAASL
TLSVTANNAS PAMAIMADVA QHPAFSAEEL DRVRTETLDG LSVSYQRPGS LAGFATAPVL
YAGSAYGHVA GGTPGSLPKI KRTDLAKAHA AYWRPDNAVL VLTGNLTPAA GFALAEKAFG
AWKKPVAPPP APPAAPTGYQ PRNVVIDLPG TGQAAVVLAK PAITRADPNY YQGIVANTVL
GVGYSSRLNQ EIRIKRGLSY GAGSSLTPQG RFGGFSARVQ TKNPSAGEVV TLTRAELSRL
AAEPASATEL TARKSVLVGN FGRDLGTSEG LANILGNLAV YGVPLTEIQS YAAKVEAVSP
EEVQAFAKAK LDPAQMSVIV AGDAKAMGED LIKAAPNATV IPAAKLDLDS PTLTK
//