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Database: UniProt
Entry: A0A2I8DK38_9BURK
LinkDB: A0A2I8DK38_9BURK
Original site: A0A2I8DK38_9BURK 
ID   A0A2I8DK38_9BURK        Unreviewed;       565 AA.
AC   A0A2I8DK38;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Peptidase M56 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C2U31_16645 {ECO:0000313|EMBL:AUT47471.1};
OS   Achromobacter sp. AONIH1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT47471.1, ECO:0000313|Proteomes:UP000236176};
RN   [1] {ECO:0000313|Proteomes:UP000236176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX   PubMed=29437920;
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   MBio 9:e02011-e02017(2018).
RN   [2] {ECO:0000313|Proteomes:UP000236176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA   Segre J.A., Mullikin J.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP026124; AUT47471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I8DK38; -.
DR   KEGG; achr:C2U31_16645; -.
DR   OrthoDB; 15218at2; -.
DR   Proteomes; UP000236176; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
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:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd07341; M56_BlaR1_MecR1_like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR008756; Peptidase_M56.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR34978; POSSIBLE SENSOR-TRANSDUCER PROTEIN BLAR; 1.
DR   PANTHER; PTHR34978:SF3; SLR0241 PROTEIN; 1.
DR   Pfam; PF05569; Peptidase_M56; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..242
FT                   /note="Peptidase M56"
FT                   /evidence="ECO:0000259|Pfam:PF05569"
FT   DOMAIN          342..560
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        369
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         531
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   565 AA;  59892 MW;  9E80986844AADDEA CRC64;
     MSGLLLGGAW ALGTALPAFL WQALGIHCAM AALLSLTRPR DARLRYALCC AGLLLCAAMF
     AADVAHAYRA LPAAGPADAA SPLWSGTWPL WCAMAWLGGA ALAALRVWAG MAWLRRLLRA
     SQPWTDAAWQ ARVAGLARRM RLRREVGLRL VRGLCTPMTA GWFKPVLLVP ANLVTGMPPD
     LLEALLAHEL AHVRRHDYLV NLLQFAAEIL LFFHPTVWWL SRRIRIERER IADDMAAALI
     GQPRRLALAL NALSQDADAA PAPVAPAARD GDLLDRIRRL TRPDSLPARR AVAMPALAAM
     LAVAIAGAGV QAGPADDGRA DAARRALAQL PGIDALIQSS GASHVLVLDA RSGDTLVGVA
     ENEAVPIASL TKLMTAMVLL DAAPDLSQPV RIDERDAEAA RGGAWQLPVG AVAPLDTMLK
     LALMSSDNRA AHALARSYPG GEAAFARALR RKVAALGLEH ARFEDAMGIS PSNRASAADI
     GRIVSAATAY PQIALDTTSL DESVGMDAGA IQYRNTNPLV GRQGWDIRLS KTATSAEAGR
     CLAMRVQAGG RELTLVLLNG RALPA
//
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