ID A0A0M4FNE9_9BACI Unreviewed; 716 AA.
AC A0A0M4FNE9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AM592_04685 {ECO:0000313|EMBL:ALC84104.1};
OS Bacillus gobiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC84104.1, ECO:0000313|Proteomes:UP000067625};
RN [1] {ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALC84104.1, ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC84104.1,
RC ECO:0000313|Proteomes:UP000067625};
RX PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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; CP012600; ALC84104.1; -; Genomic_DNA.
DR RefSeq; WP_053605984.1; NZ_CP012600.1.
DR AlphaFoldDB; A0A0M4FNE9; -.
DR STRING; 1441095.AM592_04685; -.
DR PATRIC; fig|1441095.3.peg.1030; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000067625; 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; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000067625};
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 599..659
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 716 AA; 79096 MW; 4C3BBCD2618C8CB6 CRC64;
MPTKNRFMNR GAAILSICFA LFFFVIFSRF AYIQATGKVE GEVLAAKAHE QYEKGRTISG
QRGSILDRNG EAIAEDAPSY TIIAVLDKDM TTDINHPKHV QDKAKTAKEL APILEMDEGE
ILDILNKEGR DQVEFGRAGR DISIEKKEEI EKLELPGIAF TRDSKRYYPN GMFASSLIGY
STYNNELKQM TGVMGLEKNL NNYLVKKDGF VSYESDRAGW KLPNSKDKIT PPENGKDVHL
TIDKKLQTVL EDSMSEAAKK YEPKKIMAAV MNPKTGEILA VGQRPSFDPN KRDITNYYND
IVSYPFEPGS TMKIFTLAAA VEEGVFNAAE KYHSGTYKVG KSEIGDHNNG KGWGEINFQE
GVERSSNVAF AILANEKLGA NRFNQYLRKF HFYDKTGVDM PGEAESTINF KYDIEKVTNS
FGQGSAITPI QQLQAATAIA NNGKMMKPYV IDHITDPNNK DKTVLQNSPK SAGQPISADT
AKQVRDILEK VVTSKNGTGK PYKIDGFDIA GKTGTAQLAG DDGKLLTGHE NYIFSFLGMA
PKDDPELVVY VAVQQPKLKA TESGSAPVSS IFKPVMENGL HYLNIKPKEN AEQEKPVEKE
ESYALTDFTG MRMQTAEKQV KDEGFTPVII GDGTAVHKQS PSPETGIIAK EKVFLTSDGP
VKMPDMTGWS RRDVLNYSSL SGIHFELNGQ GFATKQSVKA GKEINGKSTV KIEFTK
//
