ID A0A178Y9R2_SINSA Unreviewed; 510 AA.
AC A0A178Y9R2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OAP44187.1};
GN ORFNames=ATB98_16080 {ECO:0000313|EMBL:OAP44187.1};
OS Sinorhizobium saheli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=36856 {ECO:0000313|EMBL:OAP44187.1, ECO:0000313|Proteomes:UP000078507};
RN [1] {ECO:0000313|EMBL:OAP44187.1, ECO:0000313|Proteomes:UP000078507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 7837 {ECO:0000313|EMBL:OAP44187.1,
RC ECO:0000313|Proteomes:UP000078507};
RA Yan H., Chen W.;
RT "Ensifer anhuiense sp. nov., an effective nitrogen fixation bacterium with
RT Glycine soja.";
RL Submitted (NOV-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:OAP44187.1}.
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DR EMBL; LNQB01000074; OAP44187.1; -; Genomic_DNA.
DR RefSeq; WP_066875609.1; NZ_WITB01000187.1.
DR AlphaFoldDB; A0A178Y9R2; -.
DR STRING; 36856.ATB98_16080; -.
DR OrthoDB; 5291989at2; -.
DR Proteomes; UP000078507; 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.
DR SUPFAM; SSF110997; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OAP44187.1};
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 Protease {ECO:0000313|EMBL:OAP44187.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078507};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 426..510
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT ACT_SITE 76
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 79
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 510 AA; 53518 MW; B1B10B9D5D1BF557 CRC64;
MKSSVVSQSA FFDLAQRPLG VLSRVVGRIV LASAVVALAL SAPAFANPKY AGIVVDAKTG
KVLYGEDADE LRYPASLTKM MTLYLTFEAL EAGRISKNTP VPFSKNASAE PPSKLGVRAG
RSITVEQAIL SLVTRSANDA ATALGELLGG SEQRFARMMT NKARALGMTR TTYRNANGLP
NAEQRTTARD QARLGIALRQ HFPQYYDYFS TRSFRFGKQT IGNHNRLLGN VRGVDGIKTG
YTRASGFNLV TSAQLDGRSI VAVVMGGTSG GARDAQMRKL VAKYMPAASR RGGGNLIAEA
PAEPVAQVAE APAEPVAQVA EATPQPAATP VAVASAAMDL PNTGPVPGMR YADEAADSVE
MAYASTKRAS DNPVLSGKLA PNTLDAQSAA LARQEPASAA VDTQITNSVA KAETSPAKAE
ARSEAKVQPQ GWVIQIGATP DKAQAMTLLG KAKEKGGKAL RNATPFTVAF SSGGAQVYRA
RFGGFDDQGM AVNACKALKK KGFACWASQQ
//
