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Database: UniProt
Entry: A0A011Q540_9LACT
LinkDB: A0A011Q540_9LACT
Original site: A0A011Q540_9LACT 
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}.
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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
//
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