ID A0A1N7KCS6_9RHOB Unreviewed; 851 AA.
AC A0A1N7KCS6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Serralysin {ECO:0000313|EMBL:SIS59398.1};
GN ORFNames=SAMN05421795_101830 {ECO:0000313|EMBL:SIS59398.1};
OS Phaeovulum vinaykumarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Phaeovulum.
OX NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS59398.1, ECO:0000313|Proteomes:UP000186098};
RN [1] {ECO:0000313|Proteomes:UP000186098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOM01000001; SIS59398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7KCS6; -.
DR STRING; 407234.SAMN05421795_101830; -.
DR Proteomes; UP000186098; Unassembled WGS sequence.
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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 6.
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; 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; 8.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF10462; Peptidase_M66; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 4.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 7.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000186098};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 170..311
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 851 AA; 87301 MW; 2EC80F9A44D33587 CRC64;
MCQMCQVASV GDDGCAFEPL YAGAVIIEVG DAAANVTTSV AIGLGDTFSG NLSYAGDVDW
VAVTLTAGTR YDISLYGDGA SPLSDPYLRV MDASGTQVGY NDDGGSGLNS YMSFVASSTG
TYYLAADSYD SRDTGTYALS IAEAAPIVPY TLDQIAEQLY SGYWGGFERH FDIAPGDTLN
VDISGLTAAG QQLAIWALQG WTDATGILFD TAPASGATVH ITMDDWDSGA YTSTQISGGL
ITSAFVNVST AWLTTSGTTL DSYSYQTYLH ELGHALGLGH AGNYNGSATY GVDNYYANDS
WQATTMSYFS QTENTYINDP AAYTMTAMPA DLIALHHLYG TPTGIRSGNT VYGENTNAGG
IYAELETLRA AGNINHAVAV TIFDQGGYDT LDLRSDTDAQ LISLIPESIN TIYGVEGMLQ
IARGTIIERL YAGSGNDTIT GNDVDNRLYG FDGADSIYGG GGHDTLYGGA GNDRLNGSYG
ADTIEGGDGT DMLWGGTWSD LLDGGADADT LSGNDGNDTL LGGTGNDILY GGAHNDVLNG
GDDDDTLYGH TGNDTLYGGG GHDTLYGGAG NDRLNGSYGA DTIEGGDGTD MLWGGTWSDR
LDGGADADTL SGNDGNDTLL GDTGNDILYG GAHNDLLNGG DDDDTLYGNT GNDTLYGGGG
HDTLYGGAGN DRLSGSYGAD TIEGGDGTDM LWGGTWSDLL DGGADADTLS GNDGNDTLLG
DTGDDVLYGG AHNDVLNGGA GVDQLVGGTG ADTFVFGATS ESTVGAADVI RDFVRGVDRI
SLTGIDANTT VAGDQAFTMI GAAAFSAAGQ LRSYISGSNT IVLGDVDGDG TADFSVILTG
SLSLAASDFL L
//
