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OMPA_SHIDY
ID   OMPA_SHIDY              Reviewed;         351 AA.
AC   P02935;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Outer membrane protein A {ECO:0000255|HAMAP-Rule:MF_00842};
DE   AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE   Flags: Precursor;
GN   Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842};
OS   Shigella dysenteriae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6283478; DOI=10.1093/nar/10.7.2367;
RA   Braun G., Cole S.T.;
RT   "The nucleotide sequence coding for major outer membrane protein OmpA of
RT   Shigella dysenteriae.";
RL   Nucleic Acids Res. 10:2367-2378(1982).
CC   -!- FUNCTION: With TolR probably plays a role in maintaining the position
CC       of the peptidoglycan cell wall in the periplasm. Acts as a porin with
CC       low permeability that allows slow penetration of small solutes; an
CC       internal gate slows down solute passage. {ECO:0000255|HAMAP-
CC       Rule:MF_00842}.
CC   -!- FUNCTION: Required for conjugation with F-type plasmids; probably
CC       serves as the mating receptor on recipient cells. {ECO:0000255|HAMAP-
CC       Rule:MF_00842}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00842}.
CC   -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC       some bacteria confer sensitivity to phage and/or colicins.
CC       {ECO:0000255|HAMAP-Rule:MF_00842}.
CC   -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC       OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
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DR   EMBL; V01344; CAA24638.1; -; Genomic_DNA.
DR   PIR; A03435; MMEBAD.
DR   RefSeq; WP_005020288.1; NZ_UAUQ01000016.1.
DR   AlphaFoldDB; P02935; -.
DR   BMRB; P02935; -.
DR   SMR; P02935; -.
DR   PRIDE; P02935; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034220; P:ion transmembrane transport; IEA:UniProtKB-UniRule.
DR   CDD; cd07185; OmpA_C-like; 1.
DR   Gene3D; 3.30.1330.60; -; 1.
DR   HAMAP; MF_00842; OmpA; 1.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR006664; OMP_bac.
DR   InterPro; IPR002368; OmpA.
DR   InterPro; IPR006665; OmpA-like.
DR   InterPro; IPR006690; OMPA-like_CS.
DR   InterPro; IPR036737; OmpA-like_sf.
DR   InterPro; IPR000498; OmpA-like_TM_dom.
DR   Pfam; PF00691; OmpA; 1.
DR   Pfam; PF01389; OmpA_membrane; 1.
DR   PRINTS; PR01021; OMPADOMAIN.
DR   PRINTS; PR01022; OUTRMMBRANEA.
DR   SUPFAM; SSF103088; SSF103088; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
DR   PROSITE; PS01068; OMPA_1; 1.
DR   PROSITE; PS51123; OMPA_2; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Conjugation; Disulfide bond; Ion transport; Membrane;
KW   Porin; Repeat; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   CHAIN           22..351
FT                   /note="Outer membrane protein A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT                   /id="PRO_0000020101"
FT   TRANSMEM        27..37
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        55..66
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        70..78
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        96..107
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        112..120
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        147..156
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        161..168
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        187..195
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   REPEAT          206..207
FT                   /note="1"
FT   REPEAT          208..209
FT                   /note="2"
FT   REPEAT          210..211
FT                   /note="3"
FT   REPEAT          212..213
FT                   /note="4"
FT   DOMAIN          215..343
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   REGION          206..213
FT                   /note="4 X 2 AA tandem repeats of A-P"
FT   SITE            73
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   SITE            164
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   DISULFID        316..328
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ   SEQUENCE   351 AA;  37741 MW;  1499AA5F5395B35B CRC64;
     MKKTAIAITV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFIDNNGP THENQLGAGA
     FGGYQVNPYV GFEMGYDWLG RMPYKGSVEN GAYKAQGVQL TAKLGYPITD DLDVYTRLGG
     MVWRADTKAH NNVTGESEKN HDTGVSPVFA GGVEWAITPE IATRLEYQWT NNIGDAHTIG
     TRPDNGLLSL GVSYRFGQGE AAPVVAPAPA PAPEVQTKHF TLKSDVLFNF NKATLKPEGQ
     AALDQLYSQL SNLDPKDGSV VVLGYTDRIG SDAYNQGLSE RRAQSVVDYL ISKGIPADKI
     SARGMGESNP VTGNTCDNVK QRAALIDCLA PDRRVEIEVK GIKDVVTQPQ A
 
 
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