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Database: UniProt
Entry: N9F0M2_ACIHA
LinkDB: N9F0M2_ACIHA
Original site: N9F0M2_ACIHA 
ID   N9F0M2_ACIHA            Unreviewed;       354 AA.
AC   N9F0M2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN   ORFNames=F927_02919 {ECO:0000313|EMBL:ENW16348.1};
OS   Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW16348.1, ECO:0000313|Proteomes:UP000017667};
RN   [1] {ECO:0000313|EMBL:ENW16348.1, ECO:0000313|Proteomes:UP000017667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW16348.1,
RC   ECO:0000313|Proteomes:UP000017667};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL   Submitted (FEB-2013) 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:ENW16348.1}.
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DR   EMBL; APQQ01000030; ENW16348.1; -; Genomic_DNA.
DR   RefSeq; WP_004637598.1; NZ_KB849803.1.
DR   AlphaFoldDB; N9F0M2; -.
DR   MEROPS; S11.007; -.
DR   GeneID; 56330552; -.
DR   PATRIC; fig|1217659.3.peg.2869; -.
DR   HOGENOM; CLU_027070_0_3_6; -.
DR   Proteomes; UP000017667; 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; 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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..354
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_5004142076"
FT   DOMAIN          103..331
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        137
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   354 AA;  37323 MW;  B7940FD073A32DB1 CRC64;
     MKNAKKSVMH VLGMSILLAW SSTSFAELVV NNNSAISGNN GSASMSWSAN DASQLMNDDE
     PLDLSPVGST SVTTTLRSGG SATITSSTSP QQSVQIRDTV GYSSQPSVNA RAALVMDAQT
     GEVLFSKNTN TALPIASITK VMTAVVTADA RLNMSEEVTL QQIDFAGAGG KNSSSTLRAG
     DSMNRAELLL FALMKSENPA AAALARTYPG GRTAFYAAMN SKAKQLGMTA THFIESTGLH
     PGNVSSARDL GILVSAASQY GLIRQFSTTP TYDFNLGYRV LKSNNTNALV RNGGWNINLS
     KTGYINEAGR CVVMHTTVNS RPAVVVLLGA PSTQARNSDA TNLLTWLNTL PKRV
//
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