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Database: UniProt
Entry: A0A0V8IRS6_9BACI
LinkDB: A0A0V8IRS6_9BACI
Original site: A0A0V8IRS6_9BACI 
ID   A0A0V8IRS6_9BACI        Unreviewed;       408 AA.
AC   A0A0V8IRS6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN   ORFNames=AS030_22185 {ECO:0000313|EMBL:KSU77377.1};
OS   Fictibacillus enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU77377.1, ECO:0000313|Proteomes:UP000054099};
RN   [1] {ECO:0000313|EMBL:KSU77377.1, ECO:0000313|Proteomes:UP000054099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU77377.1,
RC   ECO:0000313|Proteomes:UP000054099};
RX   PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA   Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA   Ramana V.V., Shouche Y.S.;
RT   "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL   Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU77377.1}.
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DR   EMBL; LNQN01000010; KSU77377.1; -; Genomic_DNA.
DR   RefSeq; WP_061975856.1; NZ_KQ758624.1.
DR   AlphaFoldDB; A0A0V8IRS6; -.
DR   OrthoDB; 9791132at2; -.
DR   Proteomes; UP000054099; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR   Pfam; PF00768; Peptidase_S11; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054099};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..408
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006893398"
FT   TRANSMEM        368..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..254
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        63
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   408 AA;  45396 MW;  CDC511980F16D0AD CRC64;
     MKKFFHTIVY LCFLSGLLAP VAPVFAEQDK APHIKSNSAI LIDQKTGNVL YNKKDNKKMY
     PASVTKIVTA ILAIDSGKMD ETVTVSKNAT LTEGTRVYLN EGEQIPLRKL VEGMMVNSGN
     DAAVAIAEYL AGDVPSFADK MNEFAKKAGA THTHFVTPNG LFNPDHYTTA EDMAKITQYA
     MKNSEFRRIV KIKNLPWHVK GWDTTLVNHH RLLWDYPGTT GVKNGYVDKS KHTLVTSVSR
     DGMEFIAVVL KASTSKVAYS DTTSLFDYGF SHFQRQKISK GTLIEDPAGR KHALKEDLEV
     TLPVGEHVLK NVSASGELTL KNSAGDSLAA VQLFQPSPKK EASQMAAHSS GEATGSKLAL
     QLTTRTALFF YSGFLMLTAL MVMIRMRNKR RRALQRMRRY EKNYTFIK
//
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