ID A0A2P2EC89_9PROT Unreviewed; 580 AA.
AC A0A2P2EC89;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140};
GN Name=ftsI {ECO:0000313|EMBL:GBF58675.1};
GN ORFNames=PbB2_02363 {ECO:0000313|EMBL:GBF58675.1};
OS Candidatus Phycosocius bacilliformis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacterales incertae sedis; Phycosocius.
OX NCBI_TaxID=1445552 {ECO:0000313|EMBL:GBF58675.1, ECO:0000313|Proteomes:UP000245086};
RN [1] {ECO:0000313|EMBL:GBF58675.1, ECO:0000313|Proteomes:UP000245086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BOTRYCO-2 {ECO:0000313|EMBL:GBF58675.1,
RC ECO:0000313|Proteomes:UP000245086};
RA Tanabe Y., Yamaguchi H., Watanabe M.M.;
RT "Draft Genome Sequence of "Candidatus Phycosocius bacilliformis," an
RT Alphaproteobacterial Ectosymbiont of the Hydrocarbon-Producing Green Alga
RT Botryococcus braunii.";
RL Genome Announc. 6:e00396-18(2018).
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-A beta-lactamase family.
CC {ECO:0000256|RuleBase:RU361140}.
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:GBF58675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BFBR01000007; GBF58675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2EC89; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000245086; 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:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.450.330; -; 1.
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; IPR023650; Beta-lactam_class-A_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:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Carboxypeptidase {ECO:0000313|EMBL:GBF58675.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361140, ECO:0000313|EMBL:GBF58675.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:GBF58675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245086};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..183
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 235..524
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 61921 MW; 8D447511378C4942 CRC64;
MTDLRQPEAT VEWPRPTPRD QGGVGTMKGR TIALAVAFIA GFGLLSLRAI QIGLFRPVDE
AATAARAAAA PPSKRADLVD RNGQLLATSL VAHSLYADPK RIWDPVETAK ALRTVFPEMD
EASLIEKLSS RSRFVWIKRR LTPKQKQAVW ELAQPGLEFI EEAERIYPLG HLAGHVIGSM
HPDGSGINGI ERALNDRLTT GAGTEPVRLS LDMRVQYLVE TELAQAATAF RAEGGAAIML
DAKTGEVIAS ASWPFMDPNR PEANTPNQQN NRVTNSRFEM GSTFKVFTVA IGLEDRVITP
ESVFDARAPM RIGRELISDF HAMNKIVSVS EILAHSSNIG TVRIARSVGA PRVREFFSRL
GLMEAAGGEL LENARPILPK RWSEITAATA SFGHGIAVSP MAVAGAYAAV SNGGHYIRPT
FIARDPTVPV ASRNVISPAT STTLVKLMRD VVTNGTGKNA DAEGYEVAGK TGTAEKAGPN
GYDSNRRVSS FAGVFPARDP RYVVVFLLDE PKGYAQSGGV ATAAYAAAPS VSRIISRSAP
LLGIAPTRTL AQMDAPTGRA DPGASSPSSR PSQKAAQGEP
//
