ID A0A3T1AP07_9ACTN Unreviewed; 634 AA.
AC A0A3T1AP07;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:BBH64490.1};
GN ORFNames=ACTI_11750 {ECO:0000313|EMBL:BBH64490.1};
OS Actinoplanes sp. OR16.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=946334 {ECO:0000313|EMBL:BBH64490.1, ECO:0000313|Proteomes:UP000282692};
RN [1] {ECO:0000313|EMBL:BBH64490.1, ECO:0000313|Proteomes:UP000282692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:BBH64490.1,
RC ECO:0000313|Proteomes:UP000282692};
RA Kasai D.;
RT "Complete genome sequence of natural rubber degrading Actinoplanes sp.
RT strain OR16 isolated form botanical garden in Japan.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; AP019371; BBH64490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1AP07; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000282692; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
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; IPR007887; MecA_N.
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: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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..634
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019500903"
FT DOMAIN 27..139
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 148..307
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 357..629
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 565..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 65478 MW; CAF84F0A62ABD005 CRC64;
MRRTTAGLAA LLVLTAGGLT GCSADPPEDT VTEFLSGWQS GDLNDVGFVT ASGGAIAAPE
VLTGIRELYG DLTGQPLALT AGKTTTNGDN ATTPITVKWT LPGGVDWSYE STVRSSKAGR
DGWAVVWEPA VVQPDLAAGD KLRLRRVASE RAAIQDADGK DLVGPQKVVV IGVSPEKITS
FAELRAGLTA AFKKVDVDVD FKKLEDTVGK SDPGAFIDVV TLRRADYDKI RSQVRPLPGT
VFREETRQLA PTRAFARALL GTVDPATKED IDARPETLAV GDQAGHGGLQ QKYDDKLRGK
PGLSVVIAKE AADGETEESE VFQSEPVDGT PVKVTIDTAT QKAADTALAT EKQPSSMVAI
RVSDGAVLAV ANGPDAGGVN TALTGQVPPG STFKMISAYG VLARDVVTAD SVVDCPKTLT
VDGREFKNSH DEALGKVPFH VDFAKSCNTA FASLAPKLTS AGLQEASSAL GLGGTWDLGI
EASSGQVSDG GTATELAAAI FGQGSTVVSP LAMAAATAAV AKGQFQPPKL VLDPAPAAPG
QAGPQLDEDA LTGLRAMMRE VVTSGTGTAL KSVPGKPVHG KTGTAEFENG SDETHSWFIG
YQGDIAFAAM VQKGGAGSEA AVPIAKRFLT ELNK
//
