ID A0A0Q7DCC8_9CAUL Unreviewed; 546 AA.
AC A0A0Q7DCC8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=ASC73_00890 {ECO:0000313|EMBL:KQW72955.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW72955.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW72955.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW72955.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW72955.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW72955.1,
RC ECO:0000313|Proteomes:UP000051150};
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase M10B family.
CC {ECO:0000256|ARBA:ARBA00009490}.
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:KQW72955.1}.
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DR EMBL; LMDZ01000001; KQW72955.1; -; Genomic_DNA.
DR RefSeq; WP_056016115.1; NZ_LMDZ01000001.1.
DR AlphaFoldDB; A0A0Q7DCC8; -.
DR Proteomes; UP000051150; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 3.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051150};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..227
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 546 AA; 56365 MW; 840B80DBF9C797E1 CRC64;
MSVDPAPQFF LNADARGGLV DGKQSYTVAQ AAHQIIRGEP GWSGALGVPA AVTYAYRADA
PTTMPEDTAG FSRFNEAQIL QTELALAAWS DVANIRFMRV GIGGAGEAAY SDYATILFGN
YATGSEGSAA FAFYPGSTAS SSRAGDVWIN STKGSNLSPA MGNYGAMVLV HEIGHAIGLG
HPADYDADGS PSYSADALYY EDSRQFTVMS YFGEQNTGAN FGGRYSAAPL LDDIAAAQME
YGANMSTRTG NTVYGFNSTA DRPWFDAIAS GQKLVFAVWD AGGVDTFDFS GFSVRQLIDL
REGAFSNVGG LVGNVAVAVG ATIENAIGGT GADTINGNAA ANALTGGAGD DDLYGAAGND
SLSGGDGQDF LRGETGDDYI VGGLGFDDIH GNQGADTAYG GEGDDWVVGG QHNDLLFGEN
GMDLVYGNMG DDTMYGGVGA DVMRGGQHND IMYGEAGDDW MSGDRGDDTM WGAAGADSFH
TWGDAGVDRV MDFIRAEGDR VLVSEGASWT VAQVGADVVV SLSGGAQMVL VGVVVASLTD
GWIVAI
//