ID K0J294_AMPXN Unreviewed; 708 AA.
AC K0J294;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 Name=pbp2b {ECO:0000313|EMBL:BAM47267.1};
GN OrderedLocusNames=AXY_11350 {ECO:0000313|EMBL:BAM47267.1};
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47267.1, ECO:0000313|Proteomes:UP000006294};
RN [1] {ECO:0000313|EMBL:BAM47267.1, ECO:0000313|Proteomes:UP000006294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC Ep01 {ECO:0000313|Proteomes:UP000006294};
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; AP012050; BAM47267.1; -; Genomic_DNA.
DR AlphaFoldDB; K0J294; -.
DR STRING; 698758.AXY_11350; -.
DR KEGG; axl:AXY_11350; -.
DR PATRIC; fig|698758.3.peg.1133; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_7_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006294; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006294};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..305
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 356..679
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 80544 MW; CA040173A4D41AF2 CRC64;
MNALSNKKRN RAQIPVRLNV LFLFVFILFS VLILQLGVVQ ILNGEEARQR VNETENTTAS
IAVPRGIMYD KFGKIILDNE PERSITYTPP KNGDSSKKRL EIAEKLAKLI TMDEDFESLQ
SMVRERDKKE YWYLFNSKEA NERLTEEERE LSTSEQYRAI LNHIGPEDYN EFDWSDPYLL
NVVAIKKELD QGFELSPHTI KNEGVTEEEY ALVSENLNEL PGIDAKIDWN RVKPYGQTFS
SFIGNITTSN EGIPRENQDY YLTMGYSRND RVGTSGLEQY YESVLSGQKE IIQYTTDNNG
NILGTETVKE GKSGNDLVLT IDIEFQKEVD EIVREELENY IKSNPYENRY MSDALVAILD
PQTGDVIALS GAHYDREDNE FVDQAYRVIY DSHIPGSVVK GATMLSGYDS GVVAPGTVLL
DRPIKIAGTP TKRSWRNMHY INDKTAIIQS SNVYMFEIAM RISGAQYREN EPLRGFNSEG
FQIMRNYFHQ FGLGSRTGID LPYEATGFVG SNVQDGGLLL DFSIGQYDNY TTLQLAQYVS
TIANDGYRVS PRIVKEIRQA NGNKDTLGPV IERFGPNVLN RVTMDERYVE IIQDSFRRVA
TEGTGRGHWA NNKYNVAIKT GTAQNHFYEN GVKRETNNLT LVGYAPYEEP EIAFAIVVPR
TGIGTNQSGI HHNIGNRIVN RYFERKQEQE NANNDESNQD EAEEDLEE
//
