ID V9WSL7_9RHOB Unreviewed; 483 AA.
AC V9WSL7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Peptidase M10 serralysin {ECO:0000313|EMBL:AHD12092.1};
GN ORFNames=Gal_04388 {ECO:0000313|EMBL:AHD12092.1};
OS Phaeobacter gallaeciensis DSM 26640.
OG Plasmid pGal_F69 {ECO:0000313|EMBL:AHD12092.1,
OG ECO:0000313|Proteomes:UP000018782}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD12092.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD12092.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD12092.1,
RC ECO:0000313|Proteomes:UP000018782};
RC PLASMID=pGal_F69 {ECO:0000313|EMBL:AHD12092.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP006972; AHD12092.1; -; Genomic_DNA.
DR RefSeq; WP_024099267.1; NZ_AOQA01000018.1.
DR AlphaFoldDB; V9WSL7; -.
DR GeneID; 31848691; -.
DR KEGG; pgd:Gal_04388; -.
DR PATRIC; fig|1423144.3.peg.4404; -.
DR HOGENOM; CLU_025059_0_0_5; -.
DR OrthoDB; 733404at2; -.
DR Proteomes; UP000018782; Plasmid pGal_F69.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
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; IPR013858; Peptidase_M10B_C.
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; PF08548; Peptidase_M10_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF51120; beta-Roll; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:AHD12092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018782};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 220..434
FT /note="Peptidase M10 serralysin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08548"
FT REGION 348..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 51249 MW; 2A13BB224D959CEE CRC64;
MPTYQDYRAL LVGGADGWHE GGDVIRYHFL SSVPDYYDYD PDFGDYDVGG EYLPEGATVN
MDPAERQMML QAVTAWNEVA SLNLTPARGG VADLTFASAH FADAGLFGFI TDFPAPADLG
TTPSDAGDLW LNNSNPNQYV PGIGPVLGHT SWNTYLHELG HALGLHHPNE MPENPETPGQ
FTVMSYLPHP GEADLDTEAQ GWALTPMLWD IQAMQALYGA NTDTRTDATV YLGDGDGRGT
LAYQYGADGM TVRGGDGVAR NVSLTIWDAG GQDLIDASDV ASNSRIDLRP GQYSSIGALE
NNVAMAAAVR AEGRTLNLIE DAWGGAGHDH LIGNGAANAL VGGSGRDTLA GARGGDELSG
GQGSDRLQGG KGHDALEGGR GRDTLKGGAG QDRLDGGNGN DRMAGGRGAD VFVFSQGADV
VIDFQRDDRL DMRATTGISD FADLRNDHLE IRGTDLVIRD DNGWSLTLQD TAFDALMADD
FLF
//
