H8LSU8 (H8LSU8_CORPS) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Apolipoprotein N-acyltransferase HAMAP-Rule MF_01148
Short name=ALP N-acyltransferase HAMAP-Rule MF_01148
EC=2.3.1.- HAMAP-Rule MF_01148

Gene names

Name:	lnt HAMAP-Rule MF_01148 EMBL AFF22175.1
ORF Names:	CpP54B96_1036 EMBL AFF22175.1

Organism

Corynebacterium pseudotuberculosis P54B96 EMBL AFF22175.1

Taxonomic identifier

1117942 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium pseudotuberculosis

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Transfers the fatty acyl group on membrane lipoproteins By similarity. HAMAP-Rule MF_01148 SAAS SAAS003010
Pathway	Protein modification; lipoprotein biosynthesis (N-acyl transfer). HAMAP-Rule MF_01148 SAAS SAAS003010
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01148 SAAS SAAS003010.
Sequence similarities	Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily. HAMAP-Rule MF_01148 Contains 1 CN hydrolase domain. HAMAP-Rule MF_01148

Ontologies

Keywords
Cellular component	Cell inner membrane HAMAP-Rule MF_01148 SAAS SAAS003010 Cell membrane Membrane
Domain	Transmembrane Transmembrane helix HAMAP-Rule MF_01148 SAAS SAAS003010
Molecular function	Acyltransferase HAMAP-Rule MF_01148 SAAS SAAS003010 EMBL AFF22175.1 Transferase
PTM	Lipoprotein EMBL AFF22175.1
Gene Ontology (GO)
Biological_process	lipoprotein biosynthetic process Inferred from electronic annotation. Source: HAMAP nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acyltransferase activity Inferred from electronic annotation. Source: HAMAP hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Transmembrane	11 – 31	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	32 – 52	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	62 – 82	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	89 – 109	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	123 – 143	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	158 – 178	21	Helical; By similarity HAMAP-Rule MF_01148
	Transmembrane	189 – 209	21	Helical; By similarity HAMAP-Rule MF_01148
	Domain	217 – 506	290	CN hydrolase By similarity HAMAP-Rule MF_01148

Sequences

	Sequence		Length	Mass (Da)
	H8LSU8 [UniParc]. Last modified May 16, 2012. Version 1. Checksum: 7E3E92EEEA4B3B26	FASTA	510	54,844
	10 20 30 40 50 60 MSLSSHTMRS TLARSAIAAI AGLAVYASYA PLGWFFAAPL GLALLCGALA PWKENRPSNK 70 80 90 100 110 120 TGAFLGFIYS ITLFLLLLPW IGEFVGAMPY IALSTFLSLY SIPLGIVGVR ILRHRLGWVW 130 140 150 160 170 180 FPFVFVAVEW ARSNFPFGGF AWVRIAWGQI DGPLAGAAPW GGPALVSLLT ALVGAALWQC 190 200 210 220 230 240 VTHAAYRRQA ASVMVTVLLV AGVATLTNGQ AEDQGTVKVA AVQGNVPRLG LDFNAQRRAV 250 260 270 280 290 300 LANHVRETEK IPEQPDLVIW PENSSDVSPF SDQQAKQLVS QAVAHAQAPI LVGTITKDNV 310 320 330 340 350 360 GHRNSMVVFD PRSGVGETHN KKYLQPFGEY MPWRDFFRKL SPLVDLAGDF KPGNGNGVVH 370 380 390 400 410 420 MTAATTGKNI AVGIATCYEV AFDKAGRDAV TAGAQILTTP TNNATFGFTD MTYQQLAMSR 430 440 450 460 470 480 MRAIELDRAV VVAATSGVSA LIKPDGSVIS QTKIFQSATL EDTLPLHDTL TFSARYGTYI 490 500 510 EYALVIIGTM CALWSLFFKA KASAEEPAAS

References

[1]

Rede Paraense de Genomica e Proteomica (RPGP) Silva A., Cerdeira L., Bol E., Barbosa M.S., Muller B., Helden P.V., Santos A.R., Ramos R.T.J., Carneiro A.R., Guimaraes L.C., Aburjaile F.F., Padua U.D., Barbosa E., Fiaux K.K., Diniz C.A.A., Soares S.C., Pinto A.C., Almeida S.S. , Abreu V.A.C., Hassan S.S., Khatri G., Rahangdale S., Gupta K., Verma A.S., Ghosh P., Zambare V., Kumavath R.N., Barh D., Miyoshi A., Schneider M.P.C., Azevedo V. Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: P54B96 EMBL AFF22175.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003385 Genomic DNA. Translation: AFF22175.1.
RefSeq	YP_005375055.1. NC_017031.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AFF22175; AFF22175; CpP54B96_1036.
GeneID	11965578.
KEGG	cpp:CpP54B96_1036.
Phylogenomic databases
KO	K03820.
Enzyme and pathway databases
BioCyc	CPSE1117942:GLC0-1068-MONOMER.
UniPathway	UPA00666.
Family and domain databases
Gene3D	3.60.110.10. 1 hit.
HAMAP	MF_01148. Lnt.
InterPro	IPR004563. Apolipo_AcylTrfase. IPR003010. C-N_Hydrolase. [Graphical view]
Pfam	PF00795. CN_hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56317. Ntlse/CNhydtse. 1 hit.
TIGRFAMs	TIGR00546. lnt. 1 hit.
PROSITE	PS50263. CN_HYDROLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

H8LSU8_CORPS

Accession

Primary (citable) accession number: H8LSU8

Entry history

Integrated into UniProtKB/TrEMBL:	May 16, 2012
Last sequence update:	May 16, 2012
Last modified:	May 29, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)