ID A0A135L4B7_9BACI Unreviewed; 642 AA.
AC A0A135L4B7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=U473_06940 {ECO:0000313|EMBL:KXG43777.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG43777.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG43777.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG43777.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-2016) 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 -!- 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:KXG43777.1}.
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DR EMBL; LSKU01000001; KXG43777.1; -; Genomic_DNA.
DR RefSeq; WP_068724709.1; NZ_LSKU01000001.1.
DR AlphaFoldDB; A0A135L4B7; -.
DR STRING; 1413211.U473_06940; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000070352; 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 CDD; cd06573; PASTA; 1.
DR Gene3D; 3.30.10.20; -; 1.
DR Gene3D; 3.30.450.330; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF19; STAGE V SPORULATION PROTEIN D; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000070352};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 578..636
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 642 AA; 71006 MW; 26CCB61C712F920F CRC64;
MRRVSQVTVR KRIWLSLIIG AFLFISLIGR LGYIQLVQGK WLAEQAEELF KRDIPVEAKR
GKIYDRNGEI LAYNISAPTV VAIPVQVREP QKAAKELANI LHMSEEKIYK LITQRTLIVK
VARKISEEDA KKIKALRLPG IAIAEESRRF YPEKDFASHI LGFVGIDNQG LAGIEVVYDD
LLTGKDGAIS FPSDVTGRRM PNQSDSFTPP KDGNNLILTI DKNIQSYIER ELDQAMLTYQ
AEHSIAIAMD PNTGEILGMA SRPNYDPTNF ADYPSEIYNR NLPIWMAYEP GSTFKIITLA
AALEEDKIDL TDQFFDPGYI NVAGTDLHCW KSGGHGSETF LQVVENSCNP GFVVMGQKLG
TEKLFSYIKS FGFGAKTGID LRGEQKGILF DTNRIGPVEL ATTSFGQGVS VTPIQQVAAV
SAAINGGKLL TPHLLKEVHD PVTDEVLLIN SPEVKRQVIS PETSKKVRET LESVVANGTG
RNAYIDGYRV GGKTGTAQKI GPNGGYLANN HIVSFIGFAP ADKPEIVIYV AIDNPQGMQF
GGVVAAPIVK NILEDSLQYL GVKPRKDQLP RKDRYGIDTP YVEVPDLIGV TRNDIRNLYY
NFKLEAKGDG MRVVQQIPKP GERVEKGSTI RIYFSDNQQK GD
//
