ID A0A0F3LHA8_9CAUL Unreviewed; 496 AA.
AC A0A0F3LHA8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Beta-lactamase {ECO:0000313|EMBL:KJV42612.1};
GN ORFNames=VH88_03890 {ECO:0000313|EMBL:KJV42612.1};
OS Brevundimonas sp. KM4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV42612.1, ECO:0000313|Proteomes:UP000033583};
RN [1] {ECO:0000313|EMBL:KJV42612.1, ECO:0000313|Proteomes:UP000033583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM4 {ECO:0000313|EMBL:KJV42612.1,
RC ECO:0000313|Proteomes:UP000033583};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Brevundimonas sp. KM4.";
RL Submitted (MAR-2015) 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:KJV42612.1}.
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DR EMBL; JZRG01000007; KJV42612.1; -; Genomic_DNA.
DR RefSeq; WP_045810084.1; NZ_JZRG01000007.1.
DR AlphaFoldDB; A0A0F3LHA8; -.
DR PATRIC; fig|1628191.3.peg.2554; -.
DR Proteomes; UP000033583; Unassembled WGS sequence.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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 Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR Pfam; PF05036; SPOR; 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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002463801"
FT DOMAIN 31..258
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 419..493
FT /note="SPOR"
FT /evidence="ECO:0000259|Pfam:PF05036"
FT REGION 342..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 496 AA; 52931 MW; 579EE4DD4E6CCC17 CRC64;
MIAFLRRGLF AVLALSLVLG ANVRPIEAQT AYSAQENSRY AAIVIDAATG EVLFARNADS
RRYPASLTKM MTLYLTFEAL SQGKANVNDV LTISPRAASQ PPSKLGLAAG QTITLDNAMR
ATAVRSANDM ALAIGEHIGG SEARFTNMMT QKAAQLGMTQ TRYYTANGLP DARQVTSARD
QAILARAIMR DFPQYYSYFG LHDWAYNGRN YRNTNGLLPT GRGYDGMKTG YTNASGYNLA
ASAVRDGRRL ITIVLGGRST ASRNAHVAEL MDTGFEVERR RAQGERIQVA QTFFEQRGFG
VGSAIADAPI AYASVNDDED GVGAESTAVA YTAAPAPAAL PTRVAPAPSE RAASQRAAAT
LPPIGSAPAA SATPRAPRNV TASLNGAPAN AAVAPSTTPR RSTSSATREP ARATPRTPAG
RWAVQVGAFR EEKVASDWLT EVNRRFRDQF ATAERNVQTA GDWYRSRFVG LTETGAKSAC
ETLAARRVTC MVIGPD
//
