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Database: UniProt
Entry: A0A099GAT7_9RHOB
LinkDB: A0A099GAT7_9RHOB
Original site: A0A099GAT7_9RHOB 
ID   A0A099GAT7_9RHOB        Unreviewed;       718 AA.
AC   A0A099GAT7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN   ORFNames=IX56_15615 {ECO:0000313|EMBL:KGJ19697.1};
OS   Paracoccus sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ19697.1, ECO:0000313|Proteomes:UP000029858};
RN   [1] {ECO:0000313|EMBL:KGJ19697.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ19697.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ19697.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ19697.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) 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:KGJ19697.1}.
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DR   EMBL; JRKQ01000121; KGJ19697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099GAT7; -.
DR   Proteomes; UP000029858; 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; 2.60.120.380; -; 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; 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   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
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:UP000029858};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          152..298
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
SQ   SEQUENCE   718 AA;  75441 MW;  9355020C5EAFAEFB CRC64;
     MGLQMSARTR SAPVRLEHLD APSGTGTPIV LAPSGRFTGN VGTPYDTDWV RVDLTAGRSY
     RFEMDGLSLA DSYLELRDRR GNIVAFNDDA GRLNHSAFTY TPATSESFYL VARAYGVGTG
     SYTLTYNTTR PWTMEQIGNY LAKGFWADMS ETPRTYETGN GRPITCDLTD LGADERAVAK
     MALNAWAQVS GLRFDTTSTA GSAAQIRFTN DDQAGAYCVA DALVGNTVAR STVNIPLYWR
     DQPGEGFASY FYHTYIHEIG HALGLGHAGG YNGSATYGRD NHYANDSWQA TIMSYFSQTA
     NSSITASYGF CVTPMIADII AIQSIYDLPR NLFAGNTMWG EGCTAGGAMG LANSLMTSRQ
     AVTLTIVDQG GTDWLRLAGD TSAQMVNLQA GTVSNVYGRI GNLSIAQGTV IESVIAGRAS
     DVVRGNAADN WLCGMSGNDT LYGASGHDTL DGGAGADRLS GGRGNDLYVV DGADTLIELA
     GEGVDRVRAT VNYTLGAHFE ALLLIQSFAT YGVGNDQANT IVGNSQVNHL SGLGGNDTLF
     GMDGNDTLNG NLGADRLVGG AGDDVYIADW QDTIVEAVNG GTDTVRTSID LVLGANLERA
     IATGNAAVRI VGNGQANELI GNSAANRIVG GGGNDRMTGG GGADCFVFSP GHSGRITDFA
     DDIDLIEIRT GGSRSVTVDT VLDTARDVSG GVELTVAGGV IRIDGMIADA LRDDLILV
//
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