ID A0A0F7N3J9_9ACTN Unreviewed; 683 AA.
AC A0A0F7N3J9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:AKH81928.1};
GN ORFNames=AA958_06560 {ECO:0000313|EMBL:AKH81928.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH81928.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH81928.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH81928.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP011492; AKH81928.1; -; Genomic_DNA.
DR RefSeq; WP_047015280.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N3J9; -.
DR STRING; 444103.AA958_06560; -.
DR KEGG; strc:AA958_06560; -.
DR PATRIC; fig|444103.5.peg.1369; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.330; -; 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; 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; 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:AKH81928.1};
KW Cell division {ECO:0000313|EMBL:AKH81928.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 112..279
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 323..638
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 71803 MW; A9D29D1566FFF27B CRC64;
MTTRDSGGSS RDGGDGRDAR RRVPRPASGG RGGAARPRSR TRASTPGPRP PRPAGGGPRI
RLASPRPRLR LVSVGLTLLL LVFTARLLQV QAVDAGEYAE KAQVNRYVPM TLSAERGVIT
DRNGVELATT VDAYDITADP YLFTPEQADV KDAPRRAAEA LAPVLKADAK DLEAKLATPG
SRYVKLASKQ TPQVWDEIKK LKSESAGREA AGGRQDVLGG VFAEEQNKRV YPNGDLAAGI
LGFVNAEGEG GGGVERQHDK LLAGKDGRLV YAQSAGRRIP TADAEENPAE PGSDVELTID
RDIQWAAQTA IEKQVDASEA DRGYVIVQDT RSGEILAMAN APGFDPNDLS GATPGTLGNP
ALEDAYEPGS VNKVISMAAV LEEEAATPDT RVTVPNVLPR GGHAFHDDVE HPTWYLTLNG
VLAKSSNIGT ILAVEQLGKN QRQANKVLHS YLSDFGLGRR SGLGVAGETP GLLKPAAEWD
AAQQYTIPFG QGLSVNALQA ASVYSTVANG GVRIEPSLVR GSRGPDGRFD PAPEPEKNRV
VSQKTARTLS RMLESVVDDE EGTGVKARIP GYRAAGKTGT SNRVDPQTGR YNGYTASFAG
FAPADAPRVT VYCAIQNPTE GSYFGGQICG PVYKKVMEFA LKTLQVPPTG VEPPPMPVTF
GAGTDGTGGD GEGTDAGGVA DGG
//
