ID B2FI43_STRMK Unreviewed; 718 AA.
AC B2FI43;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Peptidyl-dipeptidase Dcp (Dipeptidyl carboxypeptidase) {ECO:0000313|EMBL:CAQ43831.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:CAQ43831.1};
GN Name=dcp {ECO:0000313|EMBL:CAQ43831.1};
GN OrderedLocusNames=Smlt0223 {ECO:0000313|EMBL:CAQ43831.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ43831.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ43831.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ43831.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM743169; CAQ43831.1; -; Genomic_DNA.
DR RefSeq; WP_012478784.1; NC_010943.1.
DR AlphaFoldDB; B2FI43; -.
DR MEROPS; M03.005; -.
DR EnsemblBacteria; CAQ43831; CAQ43831; Smlt0223.
DR GeneID; 61464226; -.
DR KEGG; sml:Smlt0223; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CAQ43831.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..718
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002777286"
FT DOMAIN 270..713
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 79557 MW; 6A52D209CDE70B24 CRC64;
MSRTVVLAAA ISLALAACSG KESTPVSDAQ KAPAQQPAEA STNPLLSAST LPFQAPQFDK
IKDSDYLPAF EEGMRQHLAD VRKIADSSEP ATFDNTIVAM ERSGETLTRV SRIFFGLVQA
DTNDARQKIQ EEVAPKLAAH QDEINLDPKL FARVKSIYDQ RDTLELDPVQ KRLVEHYYDG
LVRAGAQLSD ADKASLRKLN VEETTLSTQF HTRLVAATAA AAVVVDDKAK LAGLDEDAIN
NAANAAKERK LDGKFLLPLQ NTTQQPVLGS LSDRDQRAAV LKASETRAER GDANDTRQTV
QRLAQLRAQK AKLLGFDTFA DYQLGDQMAK TPAAALKLLT DTVPAATAKA RAEAGEIQKV
IDAQKGGFQV AASDWDFYAE QVRKAKYDLD ESQIKPYFEL DNVLQNGVFY AATQLYGITF
KPRTDIPTYN PDMKVYEVFD KDGTSLALFY TDYFKRDSKS GGAWMDVFVE QDGLTGAKPV
VYNVCNFTKP AAGQPALISF DDVTTMFHEF GHALHGMFSN VKYPSIAGTA TSRDFVEFPS
QFNEHWALDP KVFANYAKHY KTGEAMPQEL VDKILKARSF NQGYATTEYL SAALLDLAWH
TQKADAPLQD VGAFEASALK KFKVDLPQVP PRYRTTYFDH IWGGGYSAGY YAYFWAEVLD
HDAYQWFTEH GGLTAANGQE FRDKILSRGN SVELSTLYRD FRGKDPSVEP LLKFRGLK
//
