ID A0A2N0ZI81_9BACI Unreviewed; 588 AA.
AC A0A2N0ZI81;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=CWS20_09545 {ECO:0000313|EMBL:PKG29225.1};
OS Cytobacillus horneckiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=549687 {ECO:0000313|EMBL:PKG29225.1, ECO:0000313|Proteomes:UP000233343};
RN [1] {ECO:0000313|EMBL:PKG29225.1, ECO:0000313|Proteomes:UP000233343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PO1SC {ECO:0000313|Proteomes:UP000233343};
RX PubMed=19666815; DOI=10.1099/ijs.0.008979-0;
RA Vaishampayan P., Probst A., Krishnamurthi S., Ghosh S., Osman S.,
RA McDowall A., Ruckmani A., Mayilraj S., Venkateswaran K.;
RT "Bacillus horneckiae sp. nov., isolated from a spacecraft-assembly clean
RT room.";
RL Int. J. Syst. Evol. Microbiol. 60:1031-1037(2010).
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}.
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:PKG29225.1}.
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; PISD01000018; PKG29225.1; -; Genomic_DNA.
DR RefSeq; WP_066191876.1; NZ_PISD01000018.1.
DR AlphaFoldDB; A0A2N0ZI81; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000233343; Unassembled WGS sequence.
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:UP000233343}.
FT DOMAIN 56..215
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 260..567
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 588 AA; 66306 MW; C02A7D12E9CC96FE CRC64;
MWRKRAIIIV ALFITVLVGL IGRLVQIQLV DTNHFTERNI NLLEASVQQR SQEMVIDSGR
GSFLDRNGQP LTEEYKPVLI LFPFLSKMDW DIEKVSTITG ASEYALRDAV EKAKEPVTFG
TPKPLELTDK QVREINALQI PGVFAVEKKY HLANRPAEQL LGIANKDIQH RTRYDDKELP
NDALLGVTGL ERTFDEFLLA EKESKLIYHV DAKGGPLFGI NVKYVDPANP FYPLNVKTTL
DYEVQTIAEK LVDKHGIKKG GLVLLDIETN SIVAMVSRPS MNKKDPFAEG EVGTKNFMLK
KQIMGSVFKT VIAAAAIDYE LTDPNRLFDC SKKINGEPDE QYQHGMLNFS DSFAVSCNNT
FGTLAKELME IDPNIIETYA KKLSLTETVG WEGDIYHFEH FKQLYNEEQG HVFLNEEDRK
DPNFVAMTGI GQYEVRGTPL AMANMMATIA RGGEKEMVRT ASAVLYKNRT SMLQFKEMPL
EGDYIKPYTA MSLQKLLREV VVNEEGTGRL LNDLPYEVAG KSGTGQTGHS QGQEEIENKW
FAGYFPHKDP KYALVTVRLE ALENDQSTTA LFADMVTALY EFDQSQSY
//
