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PBP4_AMYLA
ID   PBP4_AMYLA              Reviewed;         381 AA.
AC   Q06317;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Penicillin-binding protein 4;
DE            Short=PBP-4;
GN   Name=pbp;
OS   Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LC411;
RX   PubMed=8440253; DOI=10.1002/j.1460-2075.1993.tb05696.x;
RA   Coque J.J.R., Liras P., Martin J.F.;
RT   "Genes for a beta-lactamase, a penicillin-binding protein and a
RT   transmembrane protein are clustered with the cephamycin biosynthetic genes
RT   in Nocardia lactamdurans.";
RL   EMBO J. 12:631-639(1993).
CC   -!- FUNCTION: Involved in cell wall biosynthesis and may also act as a
CC       sensor of external penicillins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
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DR   EMBL; Z13972; CAA78374.1; -; Genomic_DNA.
DR   PIR; S36189; S36189.
DR   AlphaFoldDB; Q06317; -.
DR   SMR; Q06317; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane; NAD;
KW   Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..381
FT                   /note="Penicillin-binding protein 4"
FT                   /id="PRO_0000195467"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        60
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299..308
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   381 AA;  40488 MW;  A3D7A80E416327EA CRC64;
     MPFDHAHWQE RFDALRTEHH VPGAALAVFV DGDLHELASG VLHRGTGVAV TTDSVFQSGS
     VAKVYTATLV MQLVDAGELR LDTRVADVLP GFAVADAEVA RTVTIGRLLS HTSGIAGDFT
     LDTGRGDDCL ARFVDACADV GQDCPPDTVI SYCSTGYAIL GRIVEVLTGQ SWDDALRDRL
     FTPLGLHQSM TLPEEALRFR VAMSHLGELG TDPEPAPVWD MLPRSAGPYG RVLITAADVV
     RFARMHLDDG VAPDGTRVLS AASAALMRQQ VAGCLDTWSF MATGWGHGWA LYDWDGVPGY
     GHDGASGGQF SYLRVVPGSG VVAALLTNGG VATSFFTDLF RELLGELAGV RMPEVFAPPA
     EPRPIDVAPL AGTYEREGGA P
 
 
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