DIVIB_STRPD
ID DIVIB_STRPD Reviewed; 382 AA.
AC Q1JG12;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Cell division protein DivIB {ECO:0000255|HAMAP-Rule:MF_00912};
GN Name=divIB {ECO:0000255|HAMAP-Rule:MF_00912};
GN OrderedLocusNames=MGAS10270_Spy1267;
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC -!- FUNCTION: Cell division protein that may be involved in stabilizing or
CC promoting the assembly of the division complex. {ECO:0000255|HAMAP-
CC Rule:MF_00912}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00912};
CC Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00912}.
CC Note=Localizes to the division septum. {ECO:0000255|HAMAP-
CC Rule:MF_00912}.
CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00912}.
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DR EMBL; CP000260; ABF34332.1; -; Genomic_DNA.
DR RefSeq; WP_020905323.1; NC_008022.1.
DR AlphaFoldDB; Q1JG12; -.
DR EnsemblBacteria; ABF34332; ABF34332; MGAS10270_Spy1267.
DR KEGG; sph:MGAS10270_Spy1267; -.
DR HOGENOM; CLU_046278_1_0_9; -.
DR OMA; YMNDGNE; -.
DR Proteomes; UP000002436; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00912; DivIB; 1.
DR InterPro; IPR026580; DivIB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR013685; POTRA_FtsQ_type.
DR Pfam; PF08478; POTRA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..382
FT /note="Cell division protein DivIB"
FT /id="PRO_0000414791"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TOPO_DOM 125..382
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT DOMAIN 125..196
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 36..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 43477 MW; A82D97026CCE1B3A CRC64;
MAKDKEKQSD DKLVLTEWQK RNIEFLKKKK QQAEEEKKLK EKLLSDKKAQ QQAQNASEAV
ELKTDEKTDS QEIESETTSK PKKTKKVRQP KEKSATQIAF QKSLPVLLGA LLLMAVSIFM
ITPYSKKKEF SVRGNHQTNL DELIKASKVK ASDYWLTLLI SPGQYERPIL RTIPWVKSVH
LSYHFPNHFL FNVIEFEIIA YAQVENGFQP ILENGKRVDK VRASELPKSF LILNLKDEKA
IQQLVKQLTT LPKKLVKNIK SVSLANSKTT ADLLLIEMHD GNVVRVPQSQ LTLKLPYYQK
LKKNLENDSI VDMEVGIYTT TQEIENQPEV PLTPEQNAAD KEGDKPGEHQ EQTDNDSETP
ANQSSPQQTP PSPETVLEQA HG