ID K7SPE8_ACIA4 Unreviewed; 649 AA.
AC K7SPE8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 OrderedLocusNames=PACID_33580 {ECO:0000313|EMBL:AFV91115.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV91115.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV91115.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
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 transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP003493; AFV91115.1; -; Genomic_DNA.
DR RefSeq; WP_015072007.1; NC_019395.1.
DR AlphaFoldDB; K7SPE8; -.
DR STRING; 1171373.PACID_33580; -.
DR KEGG; pbo:PACID_33580; -.
DR PATRIC; fig|1171373.8.peg.3304; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_025328_0_0_11; -.
DR Proteomes; UP000000214; Chromosome.
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 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; IPR007887; MecA_N.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR Pfam; PF05223; MecA_N; 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.
DR PROSITE; PS51318; TAT; 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 104..146
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 157..311
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 378..647
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 314..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 66215 MW; 94803F1FA4DA8582 CRC64;
MPQNPVVSRR TFARAAAGTT AALALGGALT GCRSSADSSV PDAARQAATK LAAGLTGGDL
KNVPLDDPTT AASDLKVIFS GMDGLRPTTT LASIAKDGDS CTATLSHTLP LGSRKWAFTS
TATLNQDGET WKAAWEPAIV HPKLGQATRL RHTRKLGERA PITGAEGKDV VVKRSVHDVG
IDKANLDKTK WEASATALAK LVKIDAKTYT ATVKAAGDQA FVVAITLREQ DIPRNIGAIA
GAQVVDRDLM LASTKTFAIG LLGTSGLADE ADVKRGKGEI QEGDMVGKSG LQLRYDDQLR
GKVGHVIAVV ARKDATASAS PAPQPTATSS ASSTASPDTP QTLFSVPATD GKPLSITLDP
DSQSKAEAAL TSVKGVAAMV AVQPGTGRIL AAANSPSAGA NAFATSGQYA PGSTFKIATT
LALLRAGLTT SSQVNCSASV TVNGRSFHNY SDYDSSYSGS IPLVDAVAQS CNTAFISQHA
KVTSAALRKA AGSLGMGTDY DTGFPSFYGK IDDTTAADVL ASDMIGQGGV LASPMAMAGV
AASVAAGKTV VPWLVEGHQP KPKATALTTK EVAELRQVMI ATVAKGSGRV LSGLATGAKT
GTAEFGESGK LRTHAWMICW TSAIAVACMV EVGESGSGTA GPLIKAFLS
//
