ID A0A077EFK4_9FLAO Unreviewed; 344 AA.
AC A0A077EFK4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Proline iminopeptidase {ECO:0000313|EMBL:AIL44305.1};
GN ORFNames=BD94_0530 {ECO:0000313|EMBL:AIL44305.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44305.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL44305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44305.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL44305.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44305.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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DR EMBL; CP007547; AIL44305.1; -; Genomic_DNA.
DR RefSeq; WP_024564647.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EFK4; -.
DR STRING; 1338011.BD94_0530; -.
DR KEGG; eao:BD94_0530; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_15_0_10; -.
DR Proteomes; UP000028933; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR NCBIfam; TIGR01250; pro_imino_pep_2; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF33; SERINE HYDROLASE-LIKE PROTEIN DDB_G0286239; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539}.
FT DOMAIN 73..324
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 318
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 344 AA; 39419 MW; B7A993DDA7AE2AD7 CRC64;
MKNIQIFILL LITATIVSCK QKESTTAGVS TADYFNYKDS VEAGGVKMIP ITTPVGNFKV
WTKRFGTNPK IKILLLHGGP AMTHEYMECF ETFFQREGFE FYEYDQLGSY YSDQPTDNRL
WNIDRFVDEV EQVRKAINAD KDNFYVLGNS WGGILAMEYA LKYQKNLKGL LVANMMASAP
EYVKYAEVLA KQMKPEILAE IRAIEAKKDY TTPRYTELLF PNYYSQHICR LPEWPDALNR
SLKHVNSTVY TLMQGPSELG MSSDAKLAKW DIKNRLHEIA TPTLMIGAKY DTMDPKAMEE
QSKLVQKGKY LYCPNGSHLA MWDDQKVFMN GVIKFIKDVD SGKL
//
