<http://linkedlifedata.com/resource/#_4531494A53320018> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://www.w3.org/1999/02/22-rdf-syntax-ns#Statement> .
<http://linkedlifedata.com/resource/#_4531494A53320018> <http://purl.uniprot.org/core/attribution> <http://linkedlifedata.com/resource/#_4531494A533200A> .
<http://linkedlifedata.com/resource/#_4531494A53320018> <http://purl.uniprot.org/core/attribution> <http://linkedlifedata.com/resource/#_4531494A53320019> .
<http://linkedlifedata.com/resource/#_4531494A53320018> <http://www.w3.org/1999/02/22-rdf-syntax-ns#subject> <http://purl.uniprot.org/SHA-384/F20C27DF73E2FDB51F4576EEAE8268A1E441D892EA1F04D1A8885A862D78701E4631E0F89A86C6ACF36A7D4DBB1273E2> .
<http://linkedlifedata.com/resource/#_4531494A53320018> <http://www.w3.org/1999/02/22-rdf-syntax-ns#predicate> <http://www.w3.org/2000/01/rdf-schema#comment> .
<http://linkedlifedata.com/resource/#_4531494A53320018> <http://www.w3.org/1999/02/22-rdf-syntax-ns#object> "Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity)." .