ID   CPTA_SALTY              Reviewed;         577 AA.
AC   Q7CPC0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phosphoethanolamine transferase CptA;
DE            EC=2.7.-.-;
GN   Name=cptA; OrderedLocusNames=STM4118;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   INDUCTION.
RX   PubMed=15681155; DOI=10.1016/j.femsim.2004.08.007;
RA   Tamayo R., Prouty A.M., Gunn J.S.;
RT   "Identification and functional analysis of Salmonella enterica serovar
RT   Typhimurium PmrA-regulated genes.";
RL   FEMS Immunol. Med. Microbiol. 43:249-258(2005).
RN   [3]
RP   FUNCTION AS A PHOSPHOETHANOLAMINE TRANSFERASE.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=15866924; DOI=10.1128/jb.187.10.3391-3399.2005;
RA   Tamayo R., Choudhury B., Septer A., Merighi M., Carlson R., Gunn J.S.;
RT   "Identification of cptA, a PmrA-regulated locus required for
RT   phosphoethanolamine modification of the Salmonella enterica serovar
RT   typhimurium lipopolysaccharide core.";
RL   J. Bacteriol. 187:3391-3399(2005).
CC   -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine moiety to the
CC       outer membrane lipopolysaccharide core. {ECO:0000269|PubMed:15866924}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:15681155}.
CC   -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family.
CC       EptC/CptA subfamily. {ECO:0000305}.
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DR   EMBL; AE006468; AAL22957.1; -; Genomic_DNA.
DR   RefSeq; NP_462998.1; NC_003197.2.
DR   RefSeq; WP_001192092.1; NC_003197.2.
DR   AlphaFoldDB; Q7CPC0; -.
DR   SMR; Q7CPC0; -.
DR   STRING; 99287.STM4118; -.
DR   PaxDb; Q7CPC0; -.
DR   PRIDE; Q7CPC0; -.
DR   EnsemblBacteria; AAL22957; AAL22957; STM4118.
DR   GeneID; 1255645; -.
DR   KEGG; stm:STM4118; -.
DR   PATRIC; fig|99287.12.peg.4340; -.
DR   HOGENOM; CLU_018534_3_3_6; -.
DR   OMA; PMYTIPF; -.
DR   PhylomeDB; Q7CPC0; -.
DR   BioCyc; SENT99287:STM4118-MON; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IBA:GO_Central.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR040423; PEA_transferase.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR30443; PTHR30443; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..577
FT                   /note="Phosphoethanolamine transferase CptA"
FT                   /id="PRO_0000383952"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   577 AA;  66207 MW;  55E0926C66D8CBEA CRC64;
     MQSTLLQTKP AFSWKALGWA LLYFWFFSTL LQAIIYLTGY SGTNGLRDSL LYSSLWLIPV
     FLFPGRIRVI AAVIGVVLWA ASLAALSYYV IYGQEFSQSV LFVMFETNAN EASEYLSQYF
     SLKIVLVALA YTVAAILLWT RLRPVYIPSP WRYLVSFALL YGLILHPIAM NTFIKHKSME
     KTLDSLASRM EPAAPWQFIT GYYQYRLQLA SLNKLLNEND ALPPLANFQD HSGDAPRTLV
     LVIGESTQRG RMSLYGYPRE TTPELDALHK TDPGLTVFNN VVTSRPYTIE ILQQALTFAD
     EKNPDWYLTK PSLMNMMKQA GYKTFWITNQ QTMTARNTML TVFSKQTDKQ FYMNQQRTQS
     AREYDSNVLA PFKAVLADPA PKKFIIVHLL GTHIKYKFRY PENQGKFDGK TDHVPPGLSS
     DELESYNDYD NANLYNDYVV ASLIKDYKAT DPNGFLLYFS DHGEEVYDTP PHKTQGRNED
     SPTRHMYTVP FLLWTSEKWQ AAHPRDFSQD VDRKYSSSEL IHTWSDLAGL TYDGYDPTRS
     ITNPQFKETT RWIGNPYKKN ALIDYDTLPY GDQVGNQ