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Database: UniProt
Entry: A0A2N0HKA3_9SPHN
LinkDB: A0A2N0HKA3_9SPHN
Original site: A0A2N0HKA3_9SPHN 
ID   A0A2N0HKA3_9SPHN        Unreviewed;       918 AA.
AC   A0A2N0HKA3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Serralysin {ECO:0000313|EMBL:PKB19380.1};
GN   ORFNames=B0I00_1612 {ECO:0000313|EMBL:PKB19380.1};
OS   Novosphingobium kunmingense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1211806 {ECO:0000313|EMBL:PKB19380.1, ECO:0000313|Proteomes:UP000232587};
RN   [1] {ECO:0000313|EMBL:PKB19380.1, ECO:0000313|Proteomes:UP000232587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12274 {ECO:0000313|EMBL:PKB19380.1,
RC   ECO:0000313|Proteomes:UP000232587};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (NOV-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}.
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:PKB19380.1}.
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DR   EMBL; PHUF01000003; PKB19380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0HKA3; -.
DR   Proteomes; UP000232587; 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   Gene3D; 2.60.120.380; -; 2.
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; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR013858; Peptidase_M10B_C.
DR   InterPro; IPR006026; Peptidase_Metallo.
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; 4.
DR   Pfam; PF08548; Peptidase_M10_C; 1.
DR   Pfam; PF04151; PPC; 2.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 3.
DR   SUPFAM; SSF89260; Collagen-binding domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000232587};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          292..443
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
SQ   SEQUENCE   918 AA;  94791 MW;  71227975B8C9A966 CRC64;
     MGLEIENALS ASPGESEDPS YGGTLFQSGY DLATYAATLD TVTADVGTTA TLSPGGSVTG
     VIDNGTDHDW YRVTLTAGQT YVFSTVLLST MIDSFMTLRD ANGTVLVEND DAISGRYHQT
     FSEILYTPSA SGTYFVDVSG FDADVGEFFV TMVGPTGDAI ASSRATTASI AVGGAVNGQI
     DSQGDHDWYA VQLVAGQSYV FATAAGAGAG IDSTIMVRGS DGTAMAFNDN AEGTFSSIRF
     TPTTSGTYYV DVGETANNAT GTYQLSAAIA PALPVYTNDE IATQLTTTYW NGSPRHFNVA
     PGGTLTVNLT ALTADGQFLA REALALWSDA TGIRFSEVAT GGQIVFDDNE AGASSSFILS
     STGIIRSASV NVSTAWLTDY GTTLRSYSLQ TYVHEIGHAL GLGHGGNYNG DANYAVDATY
     QNDAWATTVM SYFSESENTY FASLGFTTQY SVTPMLADLI AVARLYGSHA LTRTGDTVYG
     VGNNTGRAVF DAVAGQTAVS FTIIDNGGTD TVNFSGYASN ARINLNPETF SDVGGRVGNM
     AIARGTIIEN AVGGAGADVL IGNAAANRLE GGGGIDRFYG GLGNDTFVVD AQAELVFENA
     GEGTDTVETS ASYYLFANIE RLVLLGSSVI FGVGNELDNL MTGNGAENLM LGGIGNDDLR
     GGGARDSLFG EAGNDNLFGE TGIDYLAGGT GNDTLDGGDQ ADELYGEDGS DTLIGGASFD
     TDILVGGSGD DTIRGDSGLG DYDRMYGNLG NDTFYVDTPA DLIFEQIGEG SDNVIADITG
     AGFYLYDNVE NLVLAGATPF GVGNALANGL TGNSSANYLL GGAGNDTING KGGNDVLFGE
     AGADTFVFDG ASGQDVIGDF RRGEDRIQLI GSLSSFAQAQ NSFHQNGTDG AIDLGGGNFV
     VLQDVQLSTL TAADFIFG
//
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