ID A0A011Q540_9LACT Unreviewed; 721 AA.
AC A0A011Q540;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:EXJ22446.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:EXJ22446.1};
GN ORFNames=ADIAL_2032 {ECO:0000313|EMBL:EXJ22446.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22446.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ22446.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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:EXJ22446.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JANL01000042; EXJ22446.1; -; Genomic_DNA.
DR RefSeq; WP_034303099.1; NZ_JANL01000042.1.
DR AlphaFoldDB; A0A011Q540; -.
DR STRING; 1229520.ADIAL_2032; -.
DR PATRIC; fig|1229520.3.peg.1974; -.
DR eggNOG; COG0768; Bacteria.
DR Proteomes; UP000020164; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:EXJ22446.1};
KW Cell division {ECO:0000313|EMBL:EXJ22446.1};
KW Glycosyltransferase {ECO:0000313|EMBL:EXJ22446.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164};
KW Transferase {ECO:0000313|EMBL:EXJ22446.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..307
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 349..669
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 691..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 80095 MW; 808849EDDCB4DADB CRC64;
MKKPTQKRTE KHKSHIPFRL NLLFFLVFLM FASLILRLGY MQIIRADDFI AEVQRTERTT
ITGSVPRGEI FDANLRKLVG NEARATITYT RGRNVSASQM AEVAYDLAGF IEMPSVPFFE
VDSGADLTRR DLQDFFIATN QEEIRERMSD EDMQLDGGEA YQSMISYVED EELEEFSRRE
LAAAAIFRRM NAAFALSTVN IKNEDVSQDE IARVSENLDS LPGVGTGTDW VRMFPEGDML
RSIIGRVSTE RQGVPSDQVR SFLARGYTRN DRVGRTQLES QYESVLRGTR SRLDTETNSR
GEIINQIEKY SGQKGDNLIL TIDIDFQETV EQIAIDSLQE RQGLNNSIYI VAMDPRNGDV
LAMTGKTVDE NGQVRDNALG TIQAAYEMGS SVKGASILAA AMDGVLDETN NQIFDTPIRM
AGSQDIRSFF NPTGANSVMM NEVSALERSS NVYMSKLAMR MGGEFDHVQG SGLSMDAQRA
LDTQRMYFNQ FGLGVPTGID LPNESTGIAA PLVNPGQSLF FSFGQFDTYT PMQLAQYVAT
IANGGTRLAP RLVSEIRDTD PSTGGVGNLR TEIEPRILNH INVEESMMET VHQGFYAAVN
GSNGTARSHF ANTPYVSAGK TGTAEATFWR EGSDRNGEGV INTTYVGFAP FDNPEIAIAT
VVPHLPRSGR TNQESQRATR RVLDAFFGVG EFESNTQPTD NIHELEEMNE ESEQEETETE
E
//