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Database: UniProt
Entry: A0A239IVL1_9FIRM
LinkDB: A0A239IVL1_9FIRM
Original site: A0A239IVL1_9FIRM 
ID   A0A239IVL1_9FIRM        Unreviewed;       605 AA.
AC   A0A239IVL1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=SAMN05446037_103025 {ECO:0000313|EMBL:SNS96464.1};
OS   Anaerovirgula multivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Anaerovirgula.
OX   NCBI_TaxID=312168 {ECO:0000313|EMBL:SNS96464.1, ECO:0000313|Proteomes:UP000198304};
RN   [1] {ECO:0000313|EMBL:SNS96464.1, ECO:0000313|Proteomes:UP000198304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCA {ECO:0000313|EMBL:SNS96464.1,
RC   ECO:0000313|Proteomes:UP000198304};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
CC   -!- SIMILARITY: Belongs to the peptidase M56 family.
CC       {ECO:0000256|ARBA:ARBA00011075}.
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DR   EMBL; FZOJ01000030; SNS96464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239IVL1; -.
DR   OrthoDB; 9762883at2; -.
DR   Proteomes; UP000198304; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd07341; M56_BlaR1_MecR1_like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR008756; Peptidase_M56.
DR   PANTHER; PTHR34978; POSSIBLE SENSOR-TRANSDUCER PROTEIN BLAR; 1.
DR   PANTHER; PTHR34978:SF3; SLR0241 PROTEIN; 1.
DR   Pfam; PF05569; Peptidase_M56; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198304};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..314
FT                   /note="Peptidase M56"
FT                   /evidence="ECO:0000259|Pfam:PF05569"
FT   DOMAIN          339..596
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        406
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT   MOD_RES         409
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ   SEQUENCE   605 AA;  70930 MW;  280E0E082FB865F3 CRC64;
     MEPTGFLFWL ANTSFIGSIL IGIILYIKKL FHKKFHTKWH YYVWFLLVVR LVMPYAPKSP
     LSIINGFLYI RNYIVGHGIQ RTSTGDTTGI FNEAVGSIET VDFHEDYFFP MNEGFSFLIY
     RILFIIWLAG VIAITVYLVI QHIKFLKWSR KCSDINCFDL LQLFEECKTL LNIKKHINLI
     ETNEIRSPAF FGMIRPCILL PVNITEKLGL KKAKYILLHE LIHYKNRDVY INWIICFLKI
     IHWFNPIIWY GFYHMQQDRE IACDSYVLSY LETYEYRDYG RTIIAVLEEF PSPIATSFIM
     GIGSTSGCIK RRIYSIMDFK KDNRKIKLKE LAISFFIGCI LLTNPETAST MTNYSQQIDP
     TKEIIQEDLS RYFEGYEGTF VMMDMKEEQY HIFNEEMINK KVSPYSTFKI LSALIGLETG
     RLEDENTVIK WDGTNYPFED WNRDHTLASA FQYSTNWYFQ KANQYVTLQQ MKEYINILNY
     GNKRVEGDVE TFWIGGTLEI SPFQQVEFLK DFYTYEIPFT SENIDIVKKT IQLGSDGTSI
     LYGKTASSMI NDKSILGWFI GYVERGDDVY FFATKIEGND EADGRRARNI TLKILEDKKI
     FSINL
//
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