(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NMD9_YERPA

ID   A0A0E1NMD9_YERPA        Unreviewed;       269 AA.
AC   A0A0E1NMD9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   07-NOV-2018, entry version 22.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE   Flags: Precursor;
GN   Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   OrderedLocusNames=YPA_0604 {ECO:0000313|EMBL:ABG12572.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12572.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12572.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12572.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and
CC       outer membrane constriction during cell division.
CC       {ECO:0000256|HAMAP-Rule:MF_02066}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_02066}.
CC   -!- SIMILARITY: Belongs to the CpoB family. {ECO:0000256|HAMAP-
CC       Rule:MF_02066}.
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DR   EMBL; CP000308; ABG12572.1; -; Genomic_DNA.
DR   RefSeq; WP_002220051.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12572; ABG12572; YPA_0604.
DR   EnsemblBacteria; AJJ78021; AJJ78021; CH58_3463.
DR   KEGG; ypa:YPA_0604; -.
DR   PATRIC; fig|360102.15.peg.3631; -.
DR   OMA; QYWLGEV; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   HAMAP; MF_02066; CpoB; 1.
DR   InterPro; IPR034706; CpoB.
DR   InterPro; IPR014162; CpoB_C.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR032519; YbgF_tri.
DR   Pfam; PF16331; TolA_bind_tri; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   TIGRFAMs; TIGR02795; tol_pal_ybgF; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NMD9.
DR   SWISS-2DPAGE; A0A0E1NMD9.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   SIGNAL        1     23       {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   CHAIN        24    269       Cell division coordinator CpoB.
FT                                {ECO:0000256|HAMAP-Rule:MF_02066}.
FT                                /FTId=PRO_5011012943.
SQ   SEQUENCE   269 AA;  29034 MW;  BC489111C4D57935 CRC64;
     MNSNFRRHLV GLSLLVGVAV PWAATAQAPI SNVGSGSVED RVTQLERISN AHSQLLTQLQ
     QQLSDSQRDV DSLRGQIQES QYQLNQVVER QKQIYQQMES LSGGQGAQNS ASAASGATAD
     NTAAGSSGNA DAGAAASTAA PAASTGDENS DYNVAVSLAL EKKQYDQAIT AFQSFVKQYP
     KSTYQPNANY WLGQLYYNKG KKDDAAYYYA VVVKNYPKSP KSSEAMFKVG VIMQDKGQSD
     KAKAVYQQVI KQYPNTDAAK QAQKRLSAL
//

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