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Database: UniProt
Entry: N8XCE9_9GAMM
LinkDB: N8XCE9_9GAMM
Original site: N8XCE9_9GAMM 
ID   N8XCE9_9GAMM            Unreviewed;       350 AA.
AC   N8XCE9;
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=F967_02670 {ECO:0000313|EMBL:ENV05128.1};
OS   Acinetobacter sp. CIP 102637.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144669 {ECO:0000313|EMBL:ENV05128.1, ECO:0000313|Proteomes:UP000023788};
RN   [1] {ECO:0000313|EMBL:ENV05128.1, ECO:0000313|Proteomes:UP000023788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102637 {ECO:0000313|EMBL:ENV05128.1,
RC   ECO:0000313|Proteomes:UP000023788};
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 sp. CIP 102637.";
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:ENV05128.1}.
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DR   EMBL; APPG01000039; ENV05128.1; -; Genomic_DNA.
DR   AlphaFoldDB; N8XCE9; -.
DR   MEROPS; S11.007; -.
DR   PATRIC; fig|1144669.3.peg.2640; -.
DR   HOGENOM; CLU_027070_0_3_6; -.
DR   Proteomes; UP000023788; 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   Reference proteome {ECO:0000313|Proteomes:UP000023788};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..350
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_5004135800"
FT   DOMAIN          99..327
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          48..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   350 AA;  36914 MW;  EC816D9EAF5D51E7 CRC64;
     MHVLGMSILL AWSSTSFAEL VVNNSPVASG TNGSASLNWS ANDASQLMEE DEPLEISPQG
     STSVTTTLRS GGSATITSSS SPKNTVQIRD TFSNSINYSS QPSVNARAAL VMDAQTGEVL
     YSKNSNMSVP IASITKLMTA VVTADARLNM SEEITLQSID FAGAGGKNSS STLRVGDTMN
     RAEALLFALM KSENPAAAAL ARTYPGGRPA FIAAMNAKAK QLGMSSTRYA ESTGLDPHNI
     SSARDLGILV SAASQYGLIR QFSTTPAYDF NLGYRVLKSN NTNALVRNGG WNINLSKTGY
     INEAGRCVVM HTTVNSRPAV VVLLGASSSQ ARTNDATNLL NWVATLPKRI
//
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