OMPA_SERMA
ID OMPA_SERMA Reviewed; 359 AA.
AC P04845;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6092858; DOI=10.1007/bf00332766;
RA Braun G., Cole S.T.;
RT "DNA sequence analysis of the Serratia marcescens ompA gene: implications
RT for the organisation of an enterobacterial outer membrane protein.";
RL Mol. Gen. Genet. 195:321-328(1984).
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 -!- 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; X00618; CAA25254.1; -; Genomic_DNA.
DR PIR; S07298; S07298.
DR AlphaFoldDB; P04845; -.
DR SMR; P04845; -.
DR STRING; 273526.SMDB11_1037; -.
DR PRIDE; P04845; -.
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; Disulfide bond; Ion transport; Membrane; Porin;
KW Repeat; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT CHAIN 22..359
FT /note="Outer membrane protein A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT /id="PRO_0000020100"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 62..73
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 77..85
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 103..114
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 119..127
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 154..163
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 168..175
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT TRANSMEM 194..202
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REPEAT 210..211
FT /note="1"
FT REPEAT 212..213
FT /note="2"
FT REPEAT 214..215
FT /note="3"
FT REPEAT 216..217
FT /note="4"
FT REPEAT 218..219
FT /note="5"
FT DOMAIN 221..351
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 210..219
FT /note="5 X 2 AA tandem repeats of A-P"
FT SITE 80
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 171
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 322..336
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ SEQUENCE 359 AA; 38426 MW; 13992A037C19758B CRC64;
MKKTAIALAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFYGNGYQ NGIGNGPTHK
DQLGAGAFLG YQANQYLGFE LGYDWLGRMP YKGSVNNGAF KAQGVQLAAK LSYPIADDLD
IYTRLGGMVW RADSKANYGR TGQRLSDHDT GVSPLAAVGV EYALTKNWAT RLDYQFVSNI
GDAGTVGARP DNTMLSLGVS YRFGQDDVVA PAPAPAPAPV VETKRFTLKS DVLFNFNKST
LKAEGQQALD QLYTQLSSMD PKDGSVVVLG YTDAVGSDQY NQKLSEQRAQ SVVDYLVSKG
IPSDKISARG MGEADAVTGN TCGYKSGRAT KAQIVCLAPD RRVEIEVKGI KDVVTQPQG
