ID A0A1M6PSS7_9FLAO Unreviewed; 674 AA.
AC A0A1M6PSS7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05444371_1283 {ECO:0000313|EMBL:SHK10951.1};
OS Epilithonimonas mollis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=216903 {ECO:0000313|EMBL:SHK10951.1, ECO:0000313|Proteomes:UP000184498};
RN [1] {ECO:0000313|Proteomes:UP000184498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18016 {ECO:0000313|Proteomes:UP000184498};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FRAM01000001; SHK10951.1; -; Genomic_DNA.
DR RefSeq; WP_072996929.1; NZ_FRAM01000001.1.
DR AlphaFoldDB; A0A1M6PSS7; -.
DR STRING; 216903.SAMN05444371_1283; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000184498; Unassembled WGS sequence.
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 49..215
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 254..591
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 674 AA; 75658 MW; EEDC2B04E7034802 CRC64;
MKSQYLKILL ALSVIAIIFI ARLSYLQLFT DRYALNAANT SIKIEYVIPP RGVIFDRNGK
ILVGNQPAFE ISYTAALLKP DFDTLGFCKL MNMTKPEFIR TMKNIEKEKY YSRLTPMTFM
KNLSREDMAR IQELIFKYPA FSIVPRPQRQ YEINTSGNLL GYTNQVNDND IKKDSLYYLP
GDIAGKSGIE KAYEKELRGE KGMKYIQKDI RQRSIGSYKN GELDKEVVTG KDLTLTIDYD
LQRMAEEMLV NKHGAIVAID PNNGEILTMA TGPDIDPNLF TGPEKSRNLY RLANDTIYEN
KPTFDRSVQA AYPPGSTFKL LTALAAMQMG VMTDKTIFPC GGGFNYRGLR IKGHGGADPL
IPSIQVSSNC YFTYAYLNII NKYPGNPSKG VDEWKNIMNS FGVGEFLNND LAVGARGRIP
SGEFYEKRMA GIYKASGSKK DPKNWDPLAT GAVFNGMGQG DVLLTPIQMA NVVAAIANKG
WYYTPHIVKS IDGKPNPDKR FKKKHYTMVQ NPQFYNVVIQ GMEAVMLRGT GRGLMSKDFT
QLAKTGTAQV PQGKDNSIFV LIAPADKPKI VVAAVMEHAG FGATWAGPAC TTIAEKYVTG
ELKREHLYKK MITSSFMPEY KRQYIADMKR KGWYKEPPKD SAQLKRIKDS LQAIQNKKLK
KDSTKLKPLK TNAR
//
