ID Q65GT5_BACLD Unreviewed; 584 AA.
AC Q65GT5; Q62S94;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN OrderedLocusNames=BL02023 {ECO:0000313|EMBL:AAU24365.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU24365.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU24365.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP000002; AAU24365.1; -; Genomic_DNA.
DR RefSeq; WP_011198156.1; NC_006322.1.
DR AlphaFoldDB; Q65GT5; -.
DR STRING; 279010.BL02023; -.
DR KEGG; bli:BL02023; -.
DR PATRIC; fig|279010.13.peg.2916; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_3_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT DOMAIN 60..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 263..573
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 584 AA; 65615 MW; 8923115E214A7CA1 CRC64;
MKWQKRMKWV SIIISAALLF LLIRLAEIQL FFTESFSKRN VNLIQESVKQ RTEEVRISDG
RGSFLDRNGE HLSVSQKPAI VLFPFLKNQP WPAKEAAEIL NMTEDELGSK LDHAKKPVIL
TKHDGASVSK TALEKINKLK YPGVYGVYIE ETEKNRLASH TLGMTNQDPD LLRRKYPDKE
GLSISTKIGT FGMERTFDEF LLPEQDTKLL YHVDGLGNPL FGMDVKYTAD ANPFYPLQVK
TTLDKKVQQA MEDVLDDHQL DKGWAVLLDI ETNGVVAIAS KPDLNMAAQK TRQNYMLTPV
YPGSVFKTVI AAAAIENGLD HPSKTFNCNL NLYGEAGEDK GKLSLEDSFA ESCNYTFTNL
AGQLVEKNSS VIEDTAAKLG LTGRVGWEGK LYHEDEFRQF YHETAGSIWG DEKDKKVKKA
VAQTAIGQKN VKLTPLEIVN MMATIARGGE KKQVKIADQI EYKNGTLMTA FKDHELPGEK
IDQYTAQKLQ KLLRKVVTSE KGTGRRFSDL PYDVAGKSGT AQTGRTTDDK KTLYHKWFAG
YFPADKPKYA LVVVHMDTPD SKAATNAVFY DIVKKVYEIE KNQT
//
