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Database: UniProt
Entry: A0A176J1Z1_9BACI
LinkDB: A0A176J1Z1_9BACI
Original site: A0A176J1Z1_9BACI 
ID   A0A176J1Z1_9BACI        Unreviewed;       715 AA.
AC   A0A176J1Z1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=AS29_019340 {ECO:0000313|EMBL:KZZ82949.1};
OS   Bacillus sp. SJS.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ82949.1, ECO:0000313|Proteomes:UP000028527};
RN   [1] {ECO:0000313|EMBL:KZZ82949.1, ECO:0000313|Proteomes:UP000028527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJS {ECO:0000313|EMBL:KZZ82949.1,
RC   ECO:0000313|Proteomes:UP000028527};
RA   Newman J.D., Stropko S.J., Pipes S.E.;
RT   "Bacillus sp. SJS genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:KZZ82949.1}.
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DR   EMBL; JAQV02000031; KZZ82949.1; -; Genomic_DNA.
DR   RefSeq; WP_035412949.1; NZ_JAQV02000031.1.
DR   AlphaFoldDB; A0A176J1Z1; -.
DR   STRING; 1423321.AS29_019340; -.
DR   eggNOG; COG0768; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000028527; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR   CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR   Gene3D; 2.20.70.70; -; 1.
DR   Gene3D; 3.30.70.2110; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR   PROSITE; PS51178; PASTA; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028527};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          654..713
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   715 AA;  77917 MW;  257AC165F9B69B5D CRC64;
     MLKKNKNMNR GAAVLATFFA VLFFIITGRF LYIQLTGQVD GQVLAARAAQ KYEKKQILEA
     SRGSILDRNG EAIAEDTSAY TLVAILDESL TSDPKKPQHV VDKETTAEKL APILDIDTSK
     ALEILHKDAK QVEFGADGRN LSQTEKLKIE KLKLPGIAFM KNQKRFYPNG VFASDIIGYA
     QKNEENGVTT GMLGLEKSLD SYLQERDGSI KYNSDHYGWK LPGTRDEITP PDNGSDIYLT
     LDQKIQTFLE DAMNQTVKEY SPKKIMAVVA DPKTGKILAM SQRPSFNPNT RDISNFNNDI
     IGYPIEPGST MKMYTVASAI EQGVYKGSST YKSGSYKIGS KVIKDHNKTG WGSITYDEGF
     ERSSNVAMIN LAMKLGPDAY SSYMKKFGFG QKTGIDLPGE KAGTINSDSK ISLATASFGQ
     GSTATVIEQI QAATAIANGG KLMKPYLIDQ IVDADANKVI KKNEPKQISR PISEATAAQV
     RDLMGKVVTS KNGTGKPFAI EGYDVAGKTG TAQIPGDNGR YMSGKENFIF SFMGMAPKDD
     PELLVYVAVQ QPELEPTEIG SMPVSSIFKT VMQNSLQYLQ IQPEEGKGKE NDSAPKAQDP
     VMESYIGKNA KDAAKLLESS AYQPLILGSG PSVEAQSPSE RTVISKGERV FLQTGGKVKM
     PDLSGWSKRD IMKLADLLQL RVSFSGQGFS AKQSIPKGTI VSKETLLTVE LKPPS
//
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