ID A0A1V3QGW2_9FLAO Unreviewed; 531 AA.
AC A0A1V3QGW2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OOG63789.1};
GN ORFNames=B0E44_17415 {ECO:0000313|EMBL:OOG63789.1};
OS Flavobacterium sp. A45.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1945862 {ECO:0000313|EMBL:OOG63789.1, ECO:0000313|Proteomes:UP000188437};
RN [1] {ECO:0000313|EMBL:OOG63789.1, ECO:0000313|Proteomes:UP000188437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A45 {ECO:0000313|EMBL:OOG63789.1,
RC ECO:0000313|Proteomes:UP000188437};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:OOG63789.1}.
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DR EMBL; MUNX01000146; OOG63789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3QGW2; -.
DR STRING; 1945862.B0E44_17415; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000188437; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000188437};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..158
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 531 AA; 59288 MW; A51EAE3B132AC840 CRC64;
MKFDNKYLPI LIGGIFALGI FIGSLSGTPS SKAFLAKKNT KEKLNKLIDF IDNEYVDDVN
TDSIVSLTVN NILAKLDPHS VYIPPSEQAE IAETMKGDFV GIGVNFYMYN DSLAIINPVK
NGPSAKAGIK AGDRILYANK TKLFGRKLPN DSLFAALKGE AGSQIELTVY RKSERKKIKV
TIKRDVIPLK SVDAALLLDK TTGYIKINRF AETTADEFNK ALISLKKKGM KTLVVDVRDN
GGGYMEKAIA IADEFLKDKE LIVFTKSKKE STEKTYATKQ GSFESGKVFV LINENSASAS
EILAGAIQDN DRGTIVGRRS FGKGLVQREM DFNDGSAVRL TIARYYTPTG RSIQKPYSHG
NEEYFKESDS RFLHGELYKK DSIKVVDSLK YKTKKGKIVY GGGGIVPDVF VPLEAEHGAE
NVSYLLQSGI VGHFVFEQLD KNRNAFAKLT FDQFKVKINS TDLYFNAFQK YLSQNGLEVN
LEKYKTLVKR YVNAEFARQL YGDSHYYEMV LKEDAMIKVV LKQNSKPQTA K
//
