ID A0A1G8L4B2_9BRAD Unreviewed; 860 AA.
AC A0A1G8L4B2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Serralysin {ECO:0000313|EMBL:SDI50397.1};
GN ORFNames=SAMN05216338_102415 {ECO:0000313|EMBL:SDI50397.1};
OS Bradyrhizobium sp. Rc2d.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855321 {ECO:0000313|EMBL:SDI50397.1, ECO:0000313|Proteomes:UP000198770};
RN [1] {ECO:0000313|EMBL:SDI50397.1, ECO:0000313|Proteomes:UP000198770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rc2d {ECO:0000313|EMBL:SDI50397.1,
RC ECO:0000313|Proteomes:UP000198770};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNCU01000024; SDI50397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8L4B2; -.
DR STRING; 1855321.SAMN05216338_102415; -.
DR Proteomes; UP000198770; Unassembled WGS sequence.
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; 1.
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 InterPro; IPR011121; Trp-rich_dom.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF07483; W_rich_C; 3.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..195
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 860 AA; 89379 MW; 1BC987E1643F44CC CRC64;
MATAVTVTKT NNADIDGLLS GYKWSGAITY SFPDSSSDYA NPYTGGSSEP TTSGFASAPT
QMQVAINYAI GLINGYTNAN IQYAGTNGAD IMIAQSPSAN PTSYAYYPGN YASGGDVWFG
TQYNYSLAKL GNYYFVTALH ELGHAIGLKH SQETGGPANV AVPTAHDDSE YTVMSYRSYV
GASTTSGYTN EAYGYPQTYM ANDILALQTM YGANFTTQSS NTVYTWNPTT GQEFINGVGQ
PAPGGGVGGS ANRIYETVWD GGGVDTYDLS AYTTNLSINL NPGASSVFSS IQLAYLGDGH
YASGNVYNAY LYNGDARSYI DNAIGGSGND TILGNAIANT LNGGSGNDTL TGGGGNDTII
GGSGTDIALF SGNQSNYAVS YNSATQTFTL VDQRSGSPDG TDTVTGVESF QFADGTVTSA
ALISLIGPIV IEAMGTTTLT QQGANYFLNP VGGGTGPQLK YGGSAVVAGQ FSPWTLIGAE
QTATGYEIAF KQPGTDYFTI WNTDSFGNYL GNPTGIVLGT SSTLESLEAS FHQDLNGDGV
LGIPTTVIEA FGSTSLVQIG SNYYLNPTAG GSGPELMYHG AAVVTGQFNP WSLIGAEQTS
TGYEIAFKQP GTDYFTIWNT DSFGNYLGNP TGIVLGTSST LESLEASFHQ DLNGDGVLGI
PTTVIEAFGS TSLVQIGSNY YLNPTAGGSG PELMYHGAAV VTGQFNPWNL IGAEQTSTGY
EIAFKQPGTS YFTIWNTDSA GNYLGNPTGI VPGTSSALET FEPSFHQDLN GDGVIGVPAG
TAPAVFASSH NFNFDSLAAA VGTAVGDGKG GANLIDIAQA WSGGARHDPV PFSITHAQVE
HGDLPSIHVA DLHWTDFIIR
//