ID A0A0F6A0S8_9GAMM Unreviewed; 773 AA.
AC A0A0F6A0S8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=RN22_07170 {ECO:0000313|EMBL:KKD61152.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61152.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD61152.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD61152.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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:KKD61152.1}.
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DR EMBL; LASY01000029; KKD61152.1; -; Genomic_DNA.
DR RefSeq; WP_046303710.1; NZ_LASY01000029.1.
DR AlphaFoldDB; A0A0F6A0S8; -.
DR MEROPS; M04.016; -.
DR PATRIC; fig|1581149.3.peg.1992; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 2.
DR CDD; cd09597; M4_TLP; 1.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF18911; PKD_4; 2.
DR PRINTS; PR00730; THERMOLYSIN.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS50093; PKD; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..773
FT /note="PKD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002498503"
FT DOMAIN 512..574
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 635..714
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 412
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 773 AA; 84727 MW; 2DBC9019074DB86F CRC64;
MKPKFHMLSL GVAIAVTSLP SFAAQRINLE LTSFAKADNQ VEALLEGQSY IEGFSGRDLS
GNEVVRISQT YQGLPIYGES FVANKGQLGR FSGFVGSAIT GIEQDLPTTT PLISDDEALS
TLLALKGHEL YQIQHPEKQL MVWLDENDTA HLAWKVSYVV YSDKPTRPIS FIDALSGKVL
DSWEGLNHAQ STGPGGNPKT GRYHFGADYP AFDVTQSGST CYLDSENVET LDMRHQKSGG
TVHSFNCFEN SEREVNGAYS PLNDAHAFGQ IVFKMYKEWY GIAPIRQKLR MRVHYDRNYE
NAFWDGQQMT FGDGQSYFYP LVSLDVVSHE VSHGVTQQNS DLEYKNQSGG INEAFSDIAG
AAAIYYLEGS YNWKIGDRIK KGSGAMRHMD NPPLDGKSIG HAKDYYSGID VHHSSGVFNK
AFYLLATKPG WDIRKGFDIF LRANQLYWQA RSTFDHAASG VFNAASDLGY CVDDVIDAFQ
QVGVTAGGKT GEHCEDVYPV VDASFSHETK ALTAVFSNLS TGPIASYQWD FGDGRSSSQQ
SPSHTYATSG TYSVSLTVAD SKGNSDVAVN TVTVSDSDSS CSVAAWDPNK SYASGDIVSF
QGKTYKATWW STGAQPDLYP QVWSVNGDCQ TLPGDNLPPV ADFNFFASGL TISFQSTSTD
DTGIVSHTWQ FGDGTESSEK SPTHTYQQQG SYEVKLIVTD TKGLTDEKVI TIVVSNDNPT
TECYPVWQSG TVYSSGERVS HKGSAFEAKW WTQNEEPGTT GEWGVWENLG PCS
//
