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Database: UniProt
Entry: A0A077EJW7_9FLAO
LinkDB: A0A077EJW7_9FLAO
Original site: A0A077EJW7_9FLAO 
ID   A0A077EJW7_9FLAO        Unreviewed;       630 AA.
AC   A0A077EJW7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN   ORFNames=BD94_4017 {ECO:0000313|EMBL:AIL47792.1};
OS   Elizabethkingia anophelis NUHP1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL47792.1, ECO:0000313|Proteomes:UP000028933};
RN   [1] {ECO:0000313|EMBL:AIL47792.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47792.1};
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:AIL47792.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47792.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|RuleBase:RU361140};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR   EMBL; CP007547; AIL47792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077EJW7; -.
DR   STRING; 1338011.BD94_4017; -.
DR   KEGG; eao:BD94_4017; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_10; -.
DR   Proteomes; UP000028933; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          13..176
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          220..552
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          593..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  70388 MW;  3F877D5F45165A9C CRC64;
     MNAANTSIKI EYIIPQRGVI FDRNGKIMVG NQPSFEISFT QALMKSDFDT ISFCNLVGMN
     KTQFIQRIEE VKAEKYYSKL TPMTFIKDLG REDIARIQER IFKYPAFSIV SRPQRQYEIN
     TSGNLLGYTN QVNPSYIKRD STYYLPGDIA GMTGVEKSYE KQLRGVKGMK YIQKDIRLRN
     IGSYKDGKLD KQVVPGDDLT LTIDYDLQKI AEEMLVNKHG AIVAIDPNNG EILVLASGPD
     IDPNLFTGPE KNKNLYKLQV DTLYDNKPTF DRSLQAAYPP GSTFKLLTAL AGMQMGVMDE
     KTVYPCGGGF NYRGLRIKGH GGADPLIPAI RVSSNCYFSY AFISIMNKYP GDPTRGVDEW
     KKIMNSFGVG EFLNNDLAVG SKGRIPSGEF YEKRSGTKNW FSDITRNGAI FNGMGQGDVL
     LTPLQMANAV AAIANKGWYI TPHIVKLVNG KPNPDPRFKV KHKTLVDPKH FDPILKGMEQ
     VVLAGTARSL KSSDFTQLAK TGTAQVPQGK DNSIFVLIAP ADKPKIVVAA VMEHAGFGAT
     WAGPAATVIA EKYITGELKR EHLYKKMITS SFMPEYKRQW IVDLKRKGLY VEPSKQDSIQ
     KKKKTEDSLK ALRISAEQPK PQQQQNKTKN
//
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