ID   A0A081FVJ3_9GAMM        Unreviewed;       308 AA.
AC   A0A081FVJ3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Murein-DD-endopeptidase {ECO:0000313|EMBL:KEA62548.1};
DE            EC=3.4.99.- {ECO:0000313|EMBL:KEA62548.1};
GN   ORFNames=ADIMK_3439 {ECO:0000313|EMBL:KEA62548.1};
OS   Marinobacterium lacunae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA62548.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA62548.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA62548.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:KEA62548.1}.
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DR   EMBL; JMQN01000048; KEA62548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081FVJ3; -.
DR   STRING; 1232683.ADIMK_3439; -.
DR   MEROPS; S11.002; -.
DR   PATRIC; fig|1232683.4.peg.3386; -.
DR   eggNOG; COG1686; Bacteria.
DR   Proteomes; UP000028252; Unassembled WGS sequence.
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   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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, ECO:0000313|EMBL:KEA62548.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028252};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..308
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001757419"
FT   DOMAIN          32..257
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          278..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        64
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   308 AA;  34199 MW;  65615DD45CDCC1B4 CRC64;
     MMLYKSRAIL TLFLMLLAEP VLAAGLKSDP SRLHLASVNA MVTDIDTGEV LYQKNADAVV
     PIASVSKLMT ALVTLDAKLD MDERIPIRVH DSIQMKNVIS RIRLESELPR GDVLHLALMA
     SENRAATALA HAYPGGYFAF VRAMNLKAQA LGMNSTRFVE PTGLSYFNVS TARDLTKLIK
     AARNYPAVHE MTTSSKLDAR FSHPNYVLAF YNTNRLVNND EWDILLSKTG YNDEAGRCLA
     LLSRIRGHRI AMVFLDSFGK RSHIGDASRV RRWLETGDSG SVPASARRYE QEKNRGGRSA
     TLLAEKSR
//