CEMA_PHYPA
ID CEMA_PHYPA Reviewed; 439 AA.
AC Q6YXR1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Chloroplast envelope membrane protein;
GN Name=cemA {ECO:0000255|HAMAP-Rule:MF_01308};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=12954768; DOI=10.1093/nar/gkg726;
RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT evidence for the loss and relocation of rpoA from the chloroplast to the
RT nucleus.";
RL Nucleic Acids Res. 31:5324-5331(2003).
CC -!- FUNCTION: May be involved in proton extrusion. Indirectly promotes
CC efficient inorganic carbon uptake into chloroplasts.
CC {ECO:0000255|HAMAP-Rule:MF_01308}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_01308}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01308}.
CC -!- SIMILARITY: Belongs to the Cema family. {ECO:0000305}.
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DR EMBL; AP005672; BAC85040.1; -; Genomic_DNA.
DR RefSeq; NP_904190.1; NC_005087.1.
DR AlphaFoldDB; Q6YXR1; -.
DR GeneID; 2546724; -.
DR KEGG; ppp:2546724; -.
DR InParanoid; Q6YXR1; -.
DR OrthoDB; 1276845at2759; -.
DR Proteomes; UP000006727; Chloroplast.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01308; CemA; 1.
DR InterPro; IPR004282; CemA.
DR PANTHER; PTHR33650; PTHR33650; 1.
DR Pfam; PF03040; CemA; 1.
PE 3: Inferred from homology;
KW Chloroplast; Hydrogen ion transport; Ion transport; Membrane; Plastid;
KW Plastid inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..439
FT /note="Chloroplast envelope membrane protein"
FT /id="PRO_0000216656"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01308"
SQ SEQUENCE 439 AA; 52195 MW; 62555DBB52F5F8D2 CRC64;
MKFYWSQIYS WLLRTPYRSL ERAYRASKKI QHIKKNYIFY NKNIISSSRR SWQAIMLYIN
TNLNNCVFII YWSLLEYRIS LFFFDFIKTF VLIISNFFNS FFSNLISNNV IKQDLKEIKQ
MNKKLAWIEA SLNDLDMWKY YYSFSFFSKE KQKTVETSLT FVDLKKNNVT TAAYESIGLV
PRSITRTLSG FKTELTGQST SLVLQDFQIA RYQALASLQY MLFLLFIPWG FSSLLKIWFL
EPWLKNWWNT YQYQIFLNSF QEELALKRLQ QIEELVWLDK IMVNSLKEPQ SQDLNIEIHQ
KTIQLVKIYN ENSLNTLLHL LTDIVYVITL SAVFILGKQR LAILNSWIQE LFYSLSDTMK
AFSILLLTDL CIGFHSPHGW EIVIGSFLEH LGFAHNKHII SCFVSTFPVI LDTVFKYWIF
RHLNRISPSI VATYHTMNE
