ID A0A160F9R1_9BACI Unreviewed; 737 AA.
AC A0A160F9R1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=GFC29_296 {ECO:0000313|EMBL:ANB63549.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB63549.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB63549.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
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}.
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DR EMBL; CP015436; ANB63549.1; -; Genomic_DNA.
DR RefSeq; WP_044746597.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160F9R1; -.
DR KEGG; anl:GFC29_296; -.
DR PATRIC; fig|1490057.3.peg.342; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000076753; Chromosome.
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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076753};
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 596..655
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 656..713
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 718..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 82274 MW; C559E6FD56C44A09 CRC64;
MAYKKHKNTH KGAALLFGIF SLLFFVLLFR FVQLQTTGKA DGQVLAVKAE QKYEQKRTIE
AKRGTILDRN GEVLAEDTPS YTLVAVLDPK MTTDPKDPKH VVDPDRTAQK LAPLLHMEVS
EVKSILTKKA KQVEFGAQGR NISYELKKKI EALKLPGIGF IRDTKRFYPN GTFASYVIGY
AQKEEDTGKT AGAMGIEKSL NRYLHEKDGY VFYQSDKEGF RLPDTKEKIV PPDNGDEVYL
TIDQKIQTFL EDAMNQVEKQ YKPKKIIAIV VNPKTGEVLA MGTRPSFDPN KRNITNYLND
AISYPYEPGS TMKVFTLAAA INEGVYNGNE LYRSGSYRVG KNEIRDHNKV GWGVITFNEG
VQRSSNVAFA KLVKEKLGED RFLQYLHRFH FHEKTGIDLP GEGVGNILYR YPIEKLTTAF
GQGTSITPIQ QIQAATAIAN DGKMMKPYIV DRIIDPDTKK VVMQNKPEVV GEPITKETSE
KVLDILETVV TSEKGTGRPY QIEGYHVAGK TGTAQIPSPK GGYLTGYENY IFSFLGMAPK
EDPQLLMYVA VQQPKLSYTE TGAAPVSMIF NSVMKNSLQY LNIRPASEET EKTTSSKKGI
ELPSYHGWPV NEAVQDLKAK GLQPVVIGNG EKVAAQLPSA GDETIIHERV VLKTDGTATM
PDLNGWSLRD VMKAAELLQL NPSIKGSGYV IAQSIRPKTA VKANDYLIVE LAEPDKWKDR
INQQKEKKDE KKKQPVD
//
