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Database: UniProt
Entry: A0A0D6KRP5_9CYAN
LinkDB: A0A0D6KRP5_9CYAN
Original site: A0A0D6KRP5_9CYAN 
ID   A0A0D6KRP5_9CYAN        Unreviewed;       612 AA.
AC   A0A0D6KRP5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Cell division protein {ECO:0000313|EMBL:EKF02174.1};
GN   ORFNames=FDUTEX481_06897 {ECO:0000313|EMBL:EKF02174.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF02174.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF02174.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:EKF02174.1}.
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DR   EMBL; AGCR01000033; EKF02174.1; -; Genomic_DNA.
DR   RefSeq; WP_045870319.1; NZ_JH930360.1.
DR   AlphaFoldDB; A0A0D6KRP5; -.
DR   STRING; 1188.FDUTEX481_06897; -.
DR   PATRIC; fig|1188.3.peg.3984; -.
DR   HOGENOM; CLU_009289_1_2_3; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   NCBIfam; TIGR03423; pbp2_mrdA; 1.
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   4: Predicted;
KW   Cell cycle {ECO:0000313|EMBL:EKF02174.1};
KW   Cell division {ECO:0000313|EMBL:EKF02174.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..238
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          271..584
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          523..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  66844 MW;  285F289C40D0B03F CRC64;
     MDFIPSALPG SKKDTRTVGR GFQSVFLIIF TLIMTAGIDA RLAYLQIVEG PKLRQRAESN
     RIRMIPKQPE RGNIFDRNGK LLASTRYPHS VYLWPMAHTK PSWPIVAPRL EKILNTSQDE
     MEKKLKLAGA NSSSLVRIAR DISEAEITAL KEYANELPGV EINTEAVRYY PEGLALAHVL
     GYTRELTPEQ LEKRKQEGYR LGDVIGQMGV EKAYEKILRG EWGGQQVEVD GAGRPIRVLG
     EKQAKAGNDL HLTIDINLQK AADQALGKYQ GAVVAIDPNN GAVLAMASHP TFDPNIFSKQ
     KLSQKDWESV QGKDHPLVNR ALSAFPPAST FKIITASAGL ETGKFSPDTV LQTFGSLTVG
     GVTFGEWNHA GFGPLGFPRA LAMSSDTFFY QVGRRVGGPD LIAWSRKYGF GQKTGIEFPD
     EESKGLVPDE KWKQKAWKMP WTVGDTINMS IGQGALQVTP LQSAIMFSVP ANGGYRVKPH
     LLKDHEEAKS WRVSLNMKPS TIKVLRDGLR KVVSEGTGKR LDVPTIAPAS GKSGTAEAGV
     GRPNHTWFGA YAPSDKPEIV VVGFGENSGD HGGTVCGPMA LQVLEAYFQH KYPGKYQKPV
     SEGNHNGGST GD
//
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