ID   MARC_SALPA              Reviewed;         221 AA.
AC   Q5PN94;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=UPF0056 inner membrane protein MarC;
GN   Name=marC; OrderedLocusNames=SPA1334;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0056 (MarC) family. {ECO:0000305}.
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DR   EMBL; CP000026; AAV77279.1; -; Genomic_DNA.
DR   RefSeq; WP_000968972.1; NC_006511.1.
DR   AlphaFoldDB; Q5PN94; -.
DR   EnsemblBacteria; AAV77279; AAV77279; SPA1334.
DR   KEGG; spt:SPA1334; -.
DR   HOGENOM; CLU_079909_2_0_6; -.
DR   OMA; MMAIVML; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002771; Multi_antbiot-R_MarC.
DR   PANTHER; PTHR33508; PTHR33508; 1.
DR   Pfam; PF01914; MarC; 1.
DR   TIGRFAMs; TIGR00427; TIGR00427; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..221
FT                   /note="UPF0056 inner membrane protein MarC"
FT                   /id="PRO_0000343824"
FT   TOPO_DOM        1..7
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..45
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..68
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..154
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..221
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  23593 MW;  3ADA7517CC358C4A CRC64;
     MMDLFKAIGL GLVVLLPLAN PLTTVALFLG LAGNMNSAER NRQSYMASVY VFAIMMVAYY
     AGQLVMNTFG ISIPGLRIAG GVIVAFIGFR MLFPQQKAHE SPEAKSKSEE LADEPTANIA
     FVPLAMPSTA GPGTIAMIIS SASTVRHGGE FPDWVIMVAP PIIFLAVAVI LWGCLRSSGA
     IMRLVGKGGI EAISRLMGFL LVCMGVQFII NGVLEIIKTY H