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
//