ID A0A2R4C649_9BURK Unreviewed; 752 AA.
AC A0A2R4C649;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=C9I28_04585 {ECO:0000313|EMBL:AVR95075.1};
OS Pseudoduganella armeniaca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=2072590 {ECO:0000313|EMBL:AVR95075.1, ECO:0000313|Proteomes:UP000240505};
RN [1] {ECO:0000313|EMBL:AVR95075.1, ECO:0000313|Proteomes:UP000240505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZMN-3 {ECO:0000313|EMBL:AVR95075.1,
RC ECO:0000313|Proteomes:UP000240505};
RA Huang H., Ren M.;
RT "Massilia armeniaca sp. nov., isolated from desert soil.";
RL Submitted (MAR-2018) 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}.
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DR EMBL; CP028324; AVR95075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4C649; -.
DR KEGG; masz:C9I28_04585; -.
DR OrthoDB; 8607307at2; -.
DR Proteomes; UP000240505; Chromosome.
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; 2.
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; 5.
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; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 8.
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:UP000240505};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 14..176
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REGION 312..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 75038 MW; 8E41E1FC5693F266 CRC64;
MVTPSGNTNI DALAYANWNA KLGGALTLTY SFPSAAPANA TAEDRSGFAP MTSAQKEDVR
TAMAAWSAVA NITFREVASG GQLQLASNDQ GSTSAAYAYF PQPYGTSGLY LNSALWYLGA
TTPNVYRINV LVHELGHSLG LKHPGDYNAG GGGSPGPYLP GALDNSDYTI MSYYDGASKA
IDGKRPAAPM LFDVLAMQYL YGANTTWHTG NDVYTFTNAA APRCIWDAGG INALDFSACT
GATIIDLHAG TFSETAPGLH NVALAYGVAV QRAVAGAGGS TIRANDLGNV ITGGAGADVV
VGGAGNDDVA GGAGNDRLQG GGGNDTLAGG EGDDLLEGGA GNDTLDGGAG SDTAQFVLAL
AGYVGAATGT GELKFVDKLS GATVLLRDVE KLVFAGVSYT LAELQAGLAS PAREHLVAGS
FDTVGADILA GTARNDVHVV DTAGDVIVEA ADGGRDTALV KIAQAGYAWT LSENVENVMV
RGMTAGTVTG NAQANQLEGD GAANTLDGGA GDDVLDGGAG ADRLLGGAGG DLLNGGRGAD
TLQGGAGDDV YVVDDAGDVV LEMVDGGTDR VQTALALYRL DDGVEQLRFT GRGAFAGTGN
ALDNRLAGGG WNDRLDGGAG NDTLIGGAGS DTLTGGAGSD TFVLRLGGGT DVVTDFVSGT
DRLEVAAGAQ PTIVTAAAEA LTARAAALAI GPADAPYARG ASALFAVHDG TATALYSFKS
ADGNAIVGAG ELTQIAQLTG VVGVTASDFL LV
//