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Database: UniProt
Entry: A0A0Q7DCC8_9CAUL
LinkDB: A0A0Q7DCC8_9CAUL
Original site: A0A0Q7DCC8_9CAUL 
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
//
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