ID A0A1A9H0F7_HELPX Unreviewed; 156 AA. AC A0A1A9H0F7; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 28-MAR-2018, entry version 13. DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|RuleBase:RU364072}; GN Name=accB {ECO:0000313|EMBL:PNL41605.1}; GN ORFNames=AA971_07385 {ECO:0000313|EMBL:ANH43195.1}, BB384_06815 GN {ECO:0000313|EMBL:PDW82526.1}, BB423_06655 GN {ECO:0000313|EMBL:PDW36948.1}, CEP78_004295 GN {ECO:0000313|EMBL:PNL41605.1}; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210 {ECO:0000313|EMBL:ANH43195.1, ECO:0000313|Proteomes:UP000078100}; RN [1] {ECO:0000313|EMBL:ANH43195.1, ECO:0000313|Proteomes:UP000078100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L7 {ECO:0000313|EMBL:ANH43195.1, RC ECO:0000313|Proteomes:UP000078100}; RA Montano V., Didelot X., Foll M., Linz B., Reinhardt R., Suerbaum S., RA Moodley Y., Jensen J.D.; RT "Detecting global and local adaptation in a worldwide sample of RT Helicobacter pylori genomes."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PDW36948.1, ECO:0000313|Proteomes:UP000219848, ECO:0000313|Proteomes:UP000220833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22317 {ECO:0000313|EMBL:PDW36948.1, RC ECO:0000313|Proteomes:UP000220833}, and 26100 RC {ECO:0000313|EMBL:PDW82526.1, ECO:0000313|Proteomes:UP000219848}; RX PubMed=28912838; DOI=.1186/s13099-017-0201-1; RA Gutierrez-Escobar A.J., Trujillo E., Acevedo O., Bravo M.M.; RT "Phylogenomics of Colombian Helicobacter pylori isolates."; RL Gut Pathog 9:52-52(2017). RN [3] {ECO:0000313|EMBL:PNL41605.1, ECO:0000313|Proteomes:UP000198044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_299 {ECO:0000313|EMBL:PNL41605.1, RC ECO:0000313|Proteomes:UP000198044}; RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Sengamalay N., RA Ott S., Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., RA Geyer C., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A CC carboxylase complex; first, biotin carboxylase catalyzes the CC carboxylation of the carrier protein and then the transcarboxylase CC transfers the carboxyl group to form malonyl-CoA. CC {ECO:0000256|RuleBase:RU364072}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|RuleBase:RU364072}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011482; ANH43195.1; -; Genomic_DNA. DR EMBL; MBGQ01000011; PDW36948.1; -; Genomic_DNA. DR EMBL; MBHV01000011; PDW82526.1; -; Genomic_DNA. DR EMBL; NJFC02000001; PNL41605.1; -; Genomic_DNA. DR RefSeq; WP_001053815.1; NZ_PHMC01000014.1. DR ProteinModelPortal; A0A1A9H0F7; -. DR EnsemblBacteria; ANH43195; ANH43195; AA971_07385. DR PATRIC; fig|1111674.3.peg.1116; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000078100; Chromosome. DR Proteomes; UP000198044; Unassembled WGS sequence. DR Proteomes; UP000219848; Unassembled WGS sequence. DR Proteomes; UP000220833; Unassembled WGS sequence. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001249; AcCoA_biotinCC. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR PRINTS; PR01071; ACOABIOTINCC. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00531; BCCP; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. PE 4: Predicted; KW Biotin {ECO:0000256|RuleBase:RU364072}; KW Complete proteome {ECO:0000313|Proteomes:UP000078100, KW ECO:0000313|Proteomes:UP000198044, ECO:0000313|Proteomes:UP000219848, KW ECO:0000313|Proteomes:UP000220833}; KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072}; KW Fatty acid metabolism {ECO:0000256|RuleBase:RU364072}; KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364072}; KW Lipid metabolism {ECO:0000256|RuleBase:RU364072}. FT DOMAIN 78 154 Lipoyl-binding. {ECO:0000259|PROSITE: FT PS50968}. SQ SEQUENCE 156 AA; 17133 MW; 2F3B860AD53947C5 CRC64; MNLSEIEELI KEFKASDLGH LKLKHEHFEL VLDKESAYAK KSALNPAHSP APIMVEASMP SVQTPVPMVC TPIVDKKEDF VLSPMVGTFY HAPSPGAEPY VKAGDTLKKG QIVGIVEAMK IMNEIEVEYP CKVVSVEVGD AQPVEYGTKL IKVEKL //