ID B7J3H1_ACIF2 Unreviewed; 272 AA.
AC B7J3H1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=AFE_0070 {ECO:0000313|EMBL:ACK79616.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK79616.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK79616.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
CC -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and outer
CC membrane constriction during cell division. {ECO:0000256|HAMAP-
CC 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; CP001219; ACK79616.1; -; Genomic_DNA.
DR RefSeq; WP_012535773.1; NC_011761.1.
DR AlphaFoldDB; B7J3H1; -.
DR STRING; 243159.AFE_0070; -.
DR PaxDb; 243159-AFE_0070; -.
DR GeneID; 66431064; -.
DR KEGG; afr:AFE_0070; -.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_044315_2_1_6; -.
DR Proteomes; UP000001362; 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR HAMAP; MF_02066; CpoB; 1.
DR InterPro; IPR034706; CpoB.
DR InterPro; IPR014162; CpoB_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02066};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02066};
KW Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW Reference proteome {ECO:0000313|Proteomes:UP000001362};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 22..272
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009990886"
SQ SEQUENCE 272 AA; 28707 MW; 1D46B3FCBEA42552 CRC64;
MKRWHLYPVL SLLCLSPFAQ AESTGEKVLQ LQQQMAVMQG ELSSLVAVQQ ANKGSQSALA
DLLGRTQHLE QEVRDLRGEL DTKTHALQTQ QQSTAAQVQA LTAQLTGGTA ATASTSSALG
SGVAIISPAA AVASAASNTS APAVQGLGQA DYQRAFDLLR QGKYGSAVTG LQGFIQKYPQ
SSLVPDAYYW LGQAQYVLGQ NDAALKSLHV VEAQFSQSSK APEAMLRMAE IYQAIGQSGK
ARTVLSKIIS QYPSTPSAQK AEAQLQALSA GK
//