ID   A0A132BYV3_9RHOB        Unreviewed;       624 AA.
AC   A0A132BYV3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Serralysin C {ECO:0000313|EMBL:KUP93539.1};
DE            EC=3.4.24.40 {ECO:0000313|EMBL:KUP93539.1};
GN   Name=prtC_1 {ECO:0000313|EMBL:KUP93539.1};
GN   ORFNames=TRIHO_15620 {ECO:0000313|EMBL:KUP93539.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP93539.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP93539.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP93539.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-2015) 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:KUP93539.1}.
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DR   EMBL; LPUY01000049; KUP93539.1; -; Genomic_DNA.
DR   RefSeq; WP_068241795.1; NZ_LPUY01000049.1.
DR   AlphaFoldDB; A0A132BYV3; -.
DR   OrthoDB; 733404at2; -.
DR   Proteomes; UP000068382; 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; 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; 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; PF08548; Peptidase_M10_C; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; beta-Roll; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KUP93539.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068382};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          179..332
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
SQ   SEQUENCE   624 AA;  66483 MW;  62F58D0B2FAE84EA CRC64;
     MCEFCAATTV FDPARHNDSE GLRINGANFF ESGDASDNLN TGYSLPVGGS FYGALDSVGD
     RDWVAVTLEA GVTYQISQSG YWGGGGTLYD GFLRVYNSNG QQVAGNDDGR HTYDAEVNMT
     VQSGGTFYIS VGSYRDSLTG TYRLDIDSNA PTVSATEEAG VQVLADYLVD GYWEESGRDE
     RSFDVSESNE ITVNLTGLTA AGQQLARWAF EAWEMVADLQ FVEVSGAAQI TYSDDSSGAY
     ATTRTWGTEI TGVDINISQD WLTRYGTELN SYSMVAHVHE LGHALGLGHQ GYYNGGAVYG
     SNQNFVNDSW QMSVMSYFSQ QENTSVDASY GLPITAMMAD IVAIQSMYGA PGADAATAGD
     SLWGHGSDFG NYLDDVFDSF LLGGDAALGS NRNFVFTIYD SDGDDTLDLS SLSTRNTVDL
     NGGSFSDIQG RTGSLAIAED TVIENLIMGS GNDTVTGNEV DNHIELGGGH DVAHGGAGTD
     RIWGGTGTDT IYGGDDRDIL YGNSSNDVLF GEGGNDLLVG QHHNDTLNGG LGNDVLSGGH
     GADVFCFDAG SGSDRIKDFK LWQGDSLQLD RDLVEDELAL DQLISTYGQV TDGGLVLTFD
     TGDTLEFMGI FDLDSADNDI LAWV
//