ID A0A1F7WGB6_9BACT Unreviewed; 758 AA.
AC A0A1F7WGB6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A2480_01525 {ECO:0000313|EMBL:OGM01577.1};
OS Candidatus Uhrbacteria bacterium RIFOXYC2_FULL_47_19.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802424 {ECO:0000313|EMBL:OGM01577.1, ECO:0000313|Proteomes:UP000176988};
RN [1] {ECO:0000313|EMBL:OGM01577.1, ECO:0000313|Proteomes:UP000176988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGM01577.1}.
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DR EMBL; MGFG01000004; OGM01577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7WGB6; -.
DR STRING; 1802424.A2480_01525; -.
DR Proteomes; UP000176988; 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; 2.
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; 2.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
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}.
FT DOMAIN 136..349
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 511..735
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
SQ SEQUENCE 758 AA; 81678 MW; B73D1EDBC3DB1331 CRC64;
MTLAGRKFLF RTTPIVVILT AAVFLVCFRT SIAAVDDGGL AAARVQLRSV YGRRTDLQGL
FAADTWLPIK SERTVGLIGL EDWARRYGCR EHSELIWYCS GNVGASTSSG PSVLIVRSEA
LVPVRSSATG FDFSTLGSTS VFVADFDSRR VILEKDANVQ HTDAAVAKLI TAITALGSVL
SLDTVVDLAS SGQVGGTQLG VATGTKITVE DLVYASLTGS ANDAAISLAL VNSSQDAFVV
AMNDRARELG LSSTILTGPT GVESGNLTTA REAAAVLIEA MGRDPIRRAL SSSKRTVAGM
NVTNSNELLT DPNNGLYVYG GKVGYLRSSG WHLVVDMREL SGQKRLVIAL SGAPTKEALF
ADAAKLGRWV WSNYKWQVSS DTTSNLTDAA PVISSGGRPL VQSTDPSLLE ARGFLRTIYD
KRGDLKTLFD VETWRPIHSE RTGDIANLDD WAVRFGHLEY DSLWWYGTAQ AKRLLAGDIS
VIASSPRALT IRNSSLSPVR VSGTADFRPS LVTARSVFVI DVPTRKVLLA EDANRMHPVA
SITKLMTGIV AIDHGIDFEG RQTLLNDDEI GGARLRVPIG TSMYFADLMY SMLVGSANNA
AHAIGRIAGG GDLDRFVDMM NDRAAEFGLA NTNFVDPSGL DVHNVSTARE LAALALEAWD
HDQLQRICST SKYSFQAGPD EHTLINTNKL LTDANNGLIV LGGKTGYLVE SKWNLVVDLK
DSREHPVLVV VLGSDGDVNL FRDARVAAEW AWSSYRWP
//
