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
//