ID G7Z913_AZOL4 Unreviewed; 415 AA.
AC G7Z913;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CBS85960.1};
GN OrderedLocusNames=AZOLI_0591 {ECO:0000313|EMBL:CBS85960.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85960.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311868; CBS85960.1; -; Genomic_DNA.
DR RefSeq; WP_014247007.1; NC_016622.1.
DR AlphaFoldDB; G7Z913; -.
DR STRING; 862719.AZOLI_0591; -.
DR KEGG; ali:AZOLI_0591; -.
DR HOGENOM; CLU_027070_1_1_5; -.
DR Proteomes; UP000005667; Chromosome.
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 PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CBS85960.1};
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:CBS85960.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003506799"
FT DOMAIN 328..415
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 265..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 415 AA; 43893 MW; 104A6702F6C64A4D CRC64;
MGRHFLAAAA LLGMVAVGSG LSAAEALAAK AAAIVVDART GQVLIDQDAD AIVHPASLTK
MMTLYLAFDA LEDGRLSLDQ QLPVSSFAES MTPTKLGLRA GQTLKVETAI LGLVTKSAND
AAVVLAEALG GTESRFAEMM TRKARELGMR RTVYRNASGL PNMEQVTTAR DYAMLSRALM
RDHAKYYPYF SRRNFVYGGR TLANHNHLMS RYEGMDGIKT GYTVASGFNL AASAVRDGRR
LVGVVMGGKS AGSRDNKMAA LLDQAFGRPS RGRDDGPVMA SLDTTRSDAV DGEGDDDDEP
VVKARPVRAA VQMAAIPAAP ARESKAARDA GSHWGVQVGA FSSRAAGNKA VSQAVKQAPF
ILRAAKASVV EAKTGKDTVY RARLTGLDEK DARKACAVLT KHGHHCVAVS PGERG
//
