ID A0A098EXW0_9BACI Unreviewed; 722 AA.
AC A0A098EXW0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BN1002_01577 {ECO:0000313|EMBL:CEG26726.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26726.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG26726.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG26726.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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}.
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DR EMBL; CCXR01000001; CEG26726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098EXW0; -.
DR STRING; 1476857.BN1002_01577; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000042335; 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; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 586..644
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 645..704
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 691..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 79575 MW; 787F9D5AF7D1A7B1 CRC64;
MFFLFSLLFF VILYRFSVIG ITGEAAGQPL AAKAEQKHTR YATIEASRGS IMDRSGEVIA
EDTASYTLVA ILDEKMTSDP KNPKHVADPE MTAAKLSKYL NLKESEILRI LEKKKTNPKL
FQVEFGKAGR DISFQTKKEI EAEKLPGITF KRDSKRFYPN GIFSSHLVGF VERKERDNGT
YASYGKLGIE KLMNKQLTGK SGKLEYESDL WGYLLPKGKE LVTPAKNGND IYLTLDKKIQ
TFLEDALNKT VKEYNPKKII AIVADPKTGE ILAMGQRPTF EPKTREGIEK GWHNEAIEYP
FEPGSTMKIF TLAAAVNEGK FNPNEPYKSG SYQVTKRDKA IKDHNGSGWG TITYLEGVQR
SSNVAFAKIA NEKLGFEKFR EYLSKFGLDK PTGIDLPDEV SSQLRYEWPI EKITTAFGQG
TAITAIQQIQ AATAIANDGK MMKPHVIKKI TDHDTGETIE EQKPEVVSEP ISAEAAKKVR
DILETVITSP KGTGHNRYNI EGYSVAGKTG TAELSQGHGY LSGKGNYIFS FLGMAPADNP
ELIVYVAVQQ PEIDSYFKGS LPVSMIFNPV MKNSLQYLNI KPSTQEPTKT GKLSDFSGKP
AANAKKELED KGFDVVLIGN GGEVASQAPE AGATALEGEK VILKTTGDAA MPDMDGWSIR
DVMKAAHLAG LNLNFKGSGY VVKQSITKGS PISKGDHLTV QLETPRQLVG EQEEKKDPDI
KE
//
